TY  - CONF
AU  - Surudžić, Nevena
AU  - Spasojević, Dragica
AU  - Stanković, Mira
AU  - Spasojević, Milica
AU  - Elgahwash, Reyadh Gomah Amar
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2012
AB  - Natural polymers such as alginate, pectin, chitosan etc. were used as carriers for the immobilization of different types of enzymes. Among investigated enzymes, peroxidases hold a special place. Immobilized enzymes are frequently used in phenol removal reactions. In this research horseradish peroxidase was immobilized within alginate micro-beads. This natural polymer was previously oxidized with sodium periodate and modified with tyramine hydrochloride. Percent of oxidation was varied from 2.5 mol% to 10 mol%, and an increase in specific activity was noticed with increasing the oxidation percent. Immobilized peroxidases showed satisfactory stabilities after 10 days of storage. Phenol concentration in a batch reactor decreased during its oxidation with horseradish peroxidase immobilized on tyramine-alginate hydrogels.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 30th International Conference Ecological Truth and Environmental Research – EcoTER’23
T1  - Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater
EP  - 271
SP  - 267
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2012
ER  - 

@conference{
author = "Surudžić, Nevena and Spasojević, Dragica and Stanković, Mira and Spasojević, Milica and Elgahwash, Reyadh Gomah Amar and Prodanović, Radivoje and Prodanović, Olivera",
year = "2023",
abstract = "Natural polymers such as alginate, pectin, chitosan etc. were used as carriers for the immobilization of different types of enzymes. Among investigated enzymes, peroxidases hold a special place. Immobilized enzymes are frequently used in phenol removal reactions. In this research horseradish peroxidase was immobilized within alginate micro-beads. This natural polymer was previously oxidized with sodium periodate and modified with tyramine hydrochloride. Percent of oxidation was varied from 2.5 mol% to 10 mol%, and an increase in specific activity was noticed with increasing the oxidation percent. Immobilized peroxidases showed satisfactory stabilities after 10 days of storage. Phenol concentration in a batch reactor decreased during its oxidation with horseradish peroxidase immobilized on tyramine-alginate hydrogels.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "30th International Conference Ecological Truth and Environmental Research – EcoTER’23",
title = "Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater",
pages = "271-267",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2012"
}

Surudžić, N., Spasojević, D., Stanković, M., Spasojević, M., Elgahwash, R. G. A., Prodanović, R.,& Prodanović, O.. (2023). Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater. in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23
University of Belgrade, Technical Faculty in Bor., 267-271.
https://hdl.handle.net/21.15107/rcub_rimsi_2012

Surudžić N, Spasojević D, Stanković M, Spasojević M, Elgahwash RGA, Prodanović R, Prodanović O. Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater. in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23. 2023;:267-271.
https://hdl.handle.net/21.15107/rcub_rimsi_2012 .

Surudžić, Nevena, Spasojević, Dragica, Stanković, Mira, Spasojević, Milica, Elgahwash, Reyadh Gomah Amar, Prodanović, Radivoje, Prodanović, Olivera, "Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater" in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23 (2023):267-271,
https://hdl.handle.net/21.15107/rcub_rimsi_2012 .

TY  - CONF
AU  - Spasojević, Dragica
AU  - Prodanović, Olivera
AU  - Surudžić, Nevena
AU  - Đikanović, Daniela
AU  - Simonović Radosavljević, Jasna
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2011
AB  - Phenols are highly toxic organic compounds found in wastewater due to various industries’ pollution. Its removal is of great importance for human and animal health. Enzymatic wastewater treatment has several advantages over traditional methods. Enzyme immobilization onto solid carriers enables its reusability and lowers the cost of treatment. In this work, immobilized horseradish peroxidase on chemically modified alginate hydrogel was tested for phenol removal. The reusability of the tested immobilizate was monitored in repeated cycles. After five consecutive cycles, the remaining activity of the immobilized enzyme was 54%. The obtained result shows the potential for using this immobilizate for wastewater treatment.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 30th International Conference Ecological Truth and Environmental Research – EcoTER’23
T1  - Wastewater treatment by aminated peroxidase in alginate hydrogel
EP  - 275
SP  - 272
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2011
ER  - 

@conference{
author = "Spasojević, Dragica and Prodanović, Olivera and Surudžić, Nevena and Đikanović, Daniela and Simonović Radosavljević, Jasna and Radotić, Ksenija and Prodanović, Radivoje",
year = "2023",
abstract = "Phenols are highly toxic organic compounds found in wastewater due to various industries’ pollution. Its removal is of great importance for human and animal health. Enzymatic wastewater treatment has several advantages over traditional methods. Enzyme immobilization onto solid carriers enables its reusability and lowers the cost of treatment. In this work, immobilized horseradish peroxidase on chemically modified alginate hydrogel was tested for phenol removal. The reusability of the tested immobilizate was monitored in repeated cycles. After five consecutive cycles, the remaining activity of the immobilized enzyme was 54%. The obtained result shows the potential for using this immobilizate for wastewater treatment.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "30th International Conference Ecological Truth and Environmental Research – EcoTER’23",
title = "Wastewater treatment by aminated peroxidase in alginate hydrogel",
pages = "275-272",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2011"
}

Spasojević, D., Prodanović, O., Surudžić, N., Đikanović, D., Simonović Radosavljević, J., Radotić, K.,& Prodanović, R.. (2023). Wastewater treatment by aminated peroxidase in alginate hydrogel. in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23
University of Belgrade, Technical Faculty in Bor., 272-275.
https://hdl.handle.net/21.15107/rcub_rimsi_2011

Spasojević D, Prodanović O, Surudžić N, Đikanović D, Simonović Radosavljević J, Radotić K, Prodanović R. Wastewater treatment by aminated peroxidase in alginate hydrogel. in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23. 2023;:272-275.
https://hdl.handle.net/21.15107/rcub_rimsi_2011 .

Spasojević, Dragica, Prodanović, Olivera, Surudžić, Nevena, Đikanović, Daniela, Simonović Radosavljević, Jasna, Radotić, Ksenija, Prodanović, Radivoje, "Wastewater treatment by aminated peroxidase in alginate hydrogel" in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23 (2023):272-275,
https://hdl.handle.net/21.15107/rcub_rimsi_2011 .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prodanović, Olivera
AU  - Mutavdžić, Dragosav
AU  - Šekuljica, Nataša
AU  - Jovanović, Jelena
AU  - Maksimović, Vuk
AU  - Radotić, Ksenija
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2480
AB  - In recent years, versatile peroxidase (VP) has emerged as a promising enzyme for biotechnological applications, as it can oxidize lignin without the external mediators. To gain insights into the breakdown process of artificial lignin by VP, reaction between the two was studied. Degradation products were fractionated using ultrafiltration and analyzed by RP- high performance liquid chromatography with mass detection (HPLC-MS) chromatography. Four fractions were obtained based on their molecular sizes: >10, 3–10, 1–3, and <1 kDa. Interestingly, while VP did not significantly alter the yields of these fractions, the chromatograms revealed the presence of oligomers with different molecular weights (MWs) resulting from the enzymatic activity. The VP exhibits a dual role in its enzymatic activity: both degrading and synthesizing these oligomers. This was confirmed by principal component analysis (PCA). The positive correlations were found between certain oligomers (D1 and D2, D5 and D6, as well as between D7, D10, T2, and T4), suggesting their simultaneous degradation. On the other hand, a negative correlation was found between the monomer and some oligomers (D7, D10, T2, and T4), indicating the decomposition of these oligomers into monomers. These findings shed light on the intricate interplay between VP and artificial lignin, offering valuable insights for potential applications in lignin valorization.
PB  - John Wiley and Sons Inc
T2  - Biotechnology Journal
T1  - Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions
SP  - 2300312
DO  - 10.1002/biot.202300312
ER  - 

@article{
author = "Spasojević, Dragica and Prodanović, Olivera and Mutavdžić, Dragosav and Šekuljica, Nataša and Jovanović, Jelena and Maksimović, Vuk and Radotić, Ksenija",
year = "2023",
abstract = "In recent years, versatile peroxidase (VP) has emerged as a promising enzyme for biotechnological applications, as it can oxidize lignin without the external mediators. To gain insights into the breakdown process of artificial lignin by VP, reaction between the two was studied. Degradation products were fractionated using ultrafiltration and analyzed by RP- high performance liquid chromatography with mass detection (HPLC-MS) chromatography. Four fractions were obtained based on their molecular sizes: >10, 3–10, 1–3, and <1 kDa. Interestingly, while VP did not significantly alter the yields of these fractions, the chromatograms revealed the presence of oligomers with different molecular weights (MWs) resulting from the enzymatic activity. The VP exhibits a dual role in its enzymatic activity: both degrading and synthesizing these oligomers. This was confirmed by principal component analysis (PCA). The positive correlations were found between certain oligomers (D1 and D2, D5 and D6, as well as between D7, D10, T2, and T4), suggesting their simultaneous degradation. On the other hand, a negative correlation was found between the monomer and some oligomers (D7, D10, T2, and T4), indicating the decomposition of these oligomers into monomers. These findings shed light on the intricate interplay between VP and artificial lignin, offering valuable insights for potential applications in lignin valorization.",
publisher = "John Wiley and Sons Inc",
journal = "Biotechnology Journal",
title = "Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions",
pages = "2300312",
doi = "10.1002/biot.202300312"
}

Spasojević, D., Prodanović, O., Mutavdžić, D., Šekuljica, N., Jovanović, J., Maksimović, V.,& Radotić, K.. (2023). Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions. in Biotechnology Journal
John Wiley and Sons Inc., 2300312.
https://doi.org/10.1002/biot.202300312

Spasojević D, Prodanović O, Mutavdžić D, Šekuljica N, Jovanović J, Maksimović V, Radotić K. Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions. in Biotechnology Journal. 2023;:2300312.
doi:10.1002/biot.202300312 .

Spasojević, Dragica, Prodanović, Olivera, Mutavdžić, Dragosav, Šekuljica, Nataša, Jovanović, Jelena, Maksimović, Vuk, Radotić, Ksenija, "Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions" in Biotechnology Journal (2023):2300312,
https://doi.org/10.1002/biot.202300312 . .

TY  - JOUR
AU  - Kalicanin, Nevena
AU  - Balaz, Ana Marija
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2612
AB  - The aim of this research was to prove the function of the putative opine dehydrogenase from Desulfohalobium retbaense and to characterize the enzyme in terms of functional and kinetic parameters. A putative opine dehydrogenase was identified from a metagenomic library by a sequence-based technique search of the metagenomic library, and afterward was successfully heterologously produced in Escherichia coli. In order to examine its potential for applications in the synthesis of secondary amines, first the substrate specificity of the enzyme towards different amino donors and amino acceptors was determined. The highest affinity was observed towards small amino acids, preferentially L-alanine, and when it comes to α-keto acids, pyruvate proved to be a preferential amino acceptor. The highest activity was observed at pH 6.5 in the absence of salts. The enzyme showed remarkable stability in a wide range of experimental conditions, such as broad pH stability (from 6.0–11.0 after 30 min incubation in buffers at a certain pH), stability in the presence of NaCl up to 3.0 M for 24 h, it retained 80% of the initial activity after 1 h incubation at 45°C, and 65% of the initial activity after 24 h incubation in 30% dimethyl sulfoxide.
PB  - Wiley-VCH GmbH
T2  - ChemBioChem
T1  - Heterologous Expression and Partial Characterization of a Putative Opine Dehydrogenase from a Metagenomic Sequence of Desulfohalobium retbaense
IS  - 20
IS  - e202300414
VL  - 24
DO  - 10.1002/cbic.202300414
ER  - 

@article{
author = "Kalicanin, Nevena and Balaz, Ana Marija and Prodanović, Olivera and Prodanović, Radivoje",
year = "2023",
abstract = "The aim of this research was to prove the function of the putative opine dehydrogenase from Desulfohalobium retbaense and to characterize the enzyme in terms of functional and kinetic parameters. A putative opine dehydrogenase was identified from a metagenomic library by a sequence-based technique search of the metagenomic library, and afterward was successfully heterologously produced in Escherichia coli. In order to examine its potential for applications in the synthesis of secondary amines, first the substrate specificity of the enzyme towards different amino donors and amino acceptors was determined. The highest affinity was observed towards small amino acids, preferentially L-alanine, and when it comes to α-keto acids, pyruvate proved to be a preferential amino acceptor. The highest activity was observed at pH 6.5 in the absence of salts. The enzyme showed remarkable stability in a wide range of experimental conditions, such as broad pH stability (from 6.0–11.0 after 30 min incubation in buffers at a certain pH), stability in the presence of NaCl up to 3.0 M for 24 h, it retained 80% of the initial activity after 1 h incubation at 45°C, and 65% of the initial activity after 24 h incubation in 30% dimethyl sulfoxide.",
publisher = "Wiley-VCH GmbH",
journal = "ChemBioChem",
title = "Heterologous Expression and Partial Characterization of a Putative Opine Dehydrogenase from a Metagenomic Sequence of Desulfohalobium retbaense",
number = "20, e202300414",
volume = "24",
doi = "10.1002/cbic.202300414"
}

Kalicanin, N., Balaz, A. M., Prodanović, O.,& Prodanović, R.. (2023). Heterologous Expression and Partial Characterization of a Putative Opine Dehydrogenase from a Metagenomic Sequence of Desulfohalobium retbaense. in ChemBioChem
Wiley-VCH GmbH., 24(20).
https://doi.org/10.1002/cbic.202300414

Kalicanin N, Balaz AM, Prodanović O, Prodanović R. Heterologous Expression and Partial Characterization of a Putative Opine Dehydrogenase from a Metagenomic Sequence of Desulfohalobium retbaense. in ChemBioChem. 2023;24(20).
doi:10.1002/cbic.202300414 .

Kalicanin, Nevena, Balaz, Ana Marija, Prodanović, Olivera, Prodanović, Radivoje, "Heterologous Expression and Partial Characterization of a Putative Opine Dehydrogenase from a Metagenomic Sequence of Desulfohalobium retbaense" in ChemBioChem, 24, no. 20 (2023),
https://doi.org/10.1002/cbic.202300414 . .

TY  - JOUR
AU  - Protić, Sara
AU  - Kaličanin, Nevena
AU  - Sencanski, Milan
AU  - Prodanović, Olivera
AU  - Milicevic, Jelena
AU  - Perovic, Vladimir
AU  - Paessler, Slobodan
AU  - Prodanović, Radivoje
AU  - Glisic, Sanja
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1796
AB  - Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing can be an effective option for achieving a rapid response. This study used a combined in silico virtual screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking. Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro. After the expression and purification of PLpro, gramicidin D was screened for protease inhibition in vitro and was found to be active against PLpro. The current study’s findings are significant because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable safety profile
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International  Journal of Molecular Sciences
T1  - In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D
IS  - 3
SP  - 1955
VL  - 24
DO  - 10.3390/ijms24031955
ER  - 

@article{
author = "Protić, Sara and Kaličanin, Nevena and Sencanski, Milan and Prodanović, Olivera and Milicevic, Jelena and Perovic, Vladimir and Paessler, Slobodan and Prodanović, Radivoje and Glisic, Sanja",
year = "2023",
abstract = "Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing can be an effective option for achieving a rapid response. This study used a combined in silico virtual screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking. Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro. After the expression and purification of PLpro, gramicidin D was screened for protease inhibition in vitro and was found to be active against PLpro. The current study’s findings are significant because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable safety profile",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International  Journal of Molecular Sciences",
title = "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D",
number = "3",
pages = "1955",
volume = "24",
doi = "10.3390/ijms24031955"
}

Protić, S., Kaličanin, N., Sencanski, M., Prodanović, O., Milicevic, J., Perovic, V., Paessler, S., Prodanović, R.,& Glisic, S.. (2023). In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in International  Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 24(3), 1955.
https://doi.org/10.3390/ijms24031955

Protić S, Kaličanin N, Sencanski M, Prodanović O, Milicevic J, Perovic V, Paessler S, Prodanović R, Glisic S. In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in International  Journal of Molecular Sciences. 2023;24(3):1955.
doi:10.3390/ijms24031955 .

Protić, Sara, Kaličanin, Nevena, Sencanski, Milan, Prodanović, Olivera, Milicevic, Jelena, Perovic, Vladimir, Paessler, Slobodan, Prodanović, Radivoje, Glisic, Sanja, "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D" in International  Journal of Molecular Sciences, 24, no. 3 (2023):1955,
https://doi.org/10.3390/ijms24031955 . .

TY  - CONF
AU  - Đikanović, Daniela
AU  - Prodanović, Olivera
AU  - Dragišić Maksimović, Jelena
AU  - Jovanović, Jelena
AU  - Kalauzi, Aleksandar
AU  - Spasojević, Dragica
AU  - Radotić, Ksenija
PY  - 2023
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1997
AB  - In this study, we investigated, in an in vitro system, the interaction of SiO2 (as a complex with NH4OH) with the peroxidase-catalyzed polymerization of lignin monomer into lignin model compound DHP, imitating conditions of the last step of lignin formation in the cell walls. The structure of obtained polymer was monitored using fluorescent spectroscopy and AFM 30 minutes after the start of synthesis. We studied effect of two different Si concentrations, 0.6 mM and 6 mM. Analysis of the DHP fluorescent spectra, and the application of mathematical decomposition clearly shows that structure of lignin model compound depends on Si concentration in the reaction mixture. The amount of Si affects the distribution of electrons in the DHP polymer. When silicon is present at a concentration of 6 mM, the position of the longest-wavelength APD band shifts towards shorter wavelengths compared to the position of the APD band for 0.6 mM Si. This indicates that during polymer synthesis, higher concentration of silicon may inhibit the formation of pi-electronic structures, which are responsible for electron delocalization. AFM images also show differences in the size and regularity of DHP globules.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 30th International Conference Ecological Truth and Environmental Research - EcoTER'23
T1  - Investigation of silica-lignin interaction. Application of AFM and fluorescence techniques
EP  - 98
SP  - 94
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1997
ER  - 

@conference{
author = "Đikanović, Daniela and Prodanović, Olivera and Dragišić Maksimović, Jelena and Jovanović, Jelena and Kalauzi, Aleksandar and Spasojević, Dragica and Radotić, Ksenija",
year = "2023",
abstract = "In this study, we investigated, in an in vitro system, the interaction of SiO2 (as a complex with NH4OH) with the peroxidase-catalyzed polymerization of lignin monomer into lignin model compound DHP, imitating conditions of the last step of lignin formation in the cell walls. The structure of obtained polymer was monitored using fluorescent spectroscopy and AFM 30 minutes after the start of synthesis. We studied effect of two different Si concentrations, 0.6 mM and 6 mM. Analysis of the DHP fluorescent spectra, and the application of mathematical decomposition clearly shows that structure of lignin model compound depends on Si concentration in the reaction mixture. The amount of Si affects the distribution of electrons in the DHP polymer. When silicon is present at a concentration of 6 mM, the position of the longest-wavelength APD band shifts towards shorter wavelengths compared to the position of the APD band for 0.6 mM Si. This indicates that during polymer synthesis, higher concentration of silicon may inhibit the formation of pi-electronic structures, which are responsible for electron delocalization. AFM images also show differences in the size and regularity of DHP globules.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "30th International Conference Ecological Truth and Environmental Research - EcoTER'23",
title = "Investigation of silica-lignin interaction. Application of AFM and fluorescence techniques",
pages = "98-94",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1997"
}

Đikanović, D., Prodanović, O., Dragišić Maksimović, J., Jovanović, J., Kalauzi, A., Spasojević, D.,& Radotić, K.. (2023). Investigation of silica-lignin interaction. Application of AFM and fluorescence techniques. in 30th International Conference Ecological Truth and Environmental Research - EcoTER'23
University of Belgrade, Technical Faculty in Bor., 94-98.
https://hdl.handle.net/21.15107/rcub_rimsi_1997

Đikanović D, Prodanović O, Dragišić Maksimović J, Jovanović J, Kalauzi A, Spasojević D, Radotić K. Investigation of silica-lignin interaction. Application of AFM and fluorescence techniques. in 30th International Conference Ecological Truth and Environmental Research - EcoTER'23. 2023;:94-98.
https://hdl.handle.net/21.15107/rcub_rimsi_1997 .

Đikanović, Daniela, Prodanović, Olivera, Dragišić Maksimović, Jelena, Jovanović, Jelena, Kalauzi, Aleksandar, Spasojević, Dragica, Radotić, Ksenija, "Investigation of silica-lignin interaction. Application of AFM and fluorescence techniques" in 30th International Conference Ecological Truth and Environmental Research - EcoTER'23 (2023):94-98,
https://hdl.handle.net/21.15107/rcub_rimsi_1997 .

TY  - CONF
AU  - Pantić, Nevena
AU  - Spasojević, Milica
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1774
AB  - For the purpose of immobilization, one of the most commonly used enzymes is horseradish peroxidase (HRP). Different carriers can be used as supports for the immobilization of HRP: alginate, pectin, magnetic-beads, macroporous copolymers, silicas etc. Covalent binding of an enzyme to the carrier leads to the formation of strong linkage, thus preventing the enzyme leakage. Macroporous copolymers with different porous characteristics were used for the immobilization of horseradish peroxidase by employing periodate and glutaraldehyde method. Five and 25 mg of HRP were immobilized per gram of the copolymer. Increasing the amount of added enzyme leads to the increase of specific activity of immobilized enzyme. Copolymer with the pore diameter of 297 nm showed the most promising results in terms of specific activity. Immobilized enzymes can be used for the removal of phenolic compounds from waste effluents.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 29th International Conference Ecological Truth and Environmental Research
T1  - Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal
EP  - 359
SP  - 354
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1774
ER  - 

@conference{
author = "Pantić, Nevena and Spasojević, Milica and Prokopijević, Miloš and Spasojević, Dragica and Balaž, Ana Marija and Prodanović, Radivoje and Prodanović, Olivera",
year = "2022",
abstract = "For the purpose of immobilization, one of the most commonly used enzymes is horseradish peroxidase (HRP). Different carriers can be used as supports for the immobilization of HRP: alginate, pectin, magnetic-beads, macroporous copolymers, silicas etc. Covalent binding of an enzyme to the carrier leads to the formation of strong linkage, thus preventing the enzyme leakage. Macroporous copolymers with different porous characteristics were used for the immobilization of horseradish peroxidase by employing periodate and glutaraldehyde method. Five and 25 mg of HRP were immobilized per gram of the copolymer. Increasing the amount of added enzyme leads to the increase of specific activity of immobilized enzyme. Copolymer with the pore diameter of 297 nm showed the most promising results in terms of specific activity. Immobilized enzymes can be used for the removal of phenolic compounds from waste effluents.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "29th International Conference Ecological Truth and Environmental Research",
title = "Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal",
pages = "359-354",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1774"
}

Pantić, N., Spasojević, M., Prokopijević, M., Spasojević, D., Balaž, A. M., Prodanović, R.,& Prodanović, O.. (2022). Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal. in 29th International Conference Ecological Truth and Environmental Research
University of Belgrade, Technical Faculty in Bor., 354-359.
https://hdl.handle.net/21.15107/rcub_rimsi_1774

Pantić N, Spasojević M, Prokopijević M, Spasojević D, Balaž AM, Prodanović R, Prodanović O. Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal. in 29th International Conference Ecological Truth and Environmental Research. 2022;:354-359.
https://hdl.handle.net/21.15107/rcub_rimsi_1774 .

Pantić, Nevena, Spasojević, Milica, Prokopijević, Miloš, Spasojević, Dragica, Balaž, Ana Marija, Prodanović, Radivoje, Prodanović, Olivera, "Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal" in 29th International Conference Ecological Truth and Environmental Research (2022):354-359,
https://hdl.handle.net/21.15107/rcub_rimsi_1774 .

TY  - CONF
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Pantić, Nevena
AU  - Stanković, Mira
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1767
AB  - Alginate is a natural polymer present in the cell wall of brown algae. Due to its many advantages, it
has been used extensively in the food industry, pharmacy, and biomedicine. To enhance properties,
such as stability and biodegradability, alginate is often chemically crosslinked. In this study, alginate
was crosslinked using N-hydroxysuccinimide, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
hydrochloride and tyramine hydrochloride. Horseradish peroxidase was self-immobilized within
hydrogel microbeads during the polymerization reaction. The glucose oxidase/glucose system
generates H2O2 internally, which can prevent the detrimental effect of excess peroxide. A small
amount of leaking enzyme shows potential for longer storage and reuse.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 29th International Conference Ecological Truth and Environmental Research - EcoTER'22
T1  - PREPARATION OF CROSSLINKED TYRAMINE-ALGINATE HYDROGEL USING EDC/NHS WITH SELF-IMMOBILIZED HRP
EP  - 363
SP  - 360
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1767
ER  - 

@conference{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Pantić, Nevena and Stanković, Mira and Radotić, Ksenija and Prodanović, Radivoje",
year = "2022",
abstract = "Alginate is a natural polymer present in the cell wall of brown algae. Due to its many advantages, it
has been used extensively in the food industry, pharmacy, and biomedicine. To enhance properties,
such as stability and biodegradability, alginate is often chemically crosslinked. In this study, alginate
was crosslinked using N-hydroxysuccinimide, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
hydrochloride and tyramine hydrochloride. Horseradish peroxidase was self-immobilized within
hydrogel microbeads during the polymerization reaction. The glucose oxidase/glucose system
generates H2O2 internally, which can prevent the detrimental effect of excess peroxide. A small
amount of leaking enzyme shows potential for longer storage and reuse.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "29th International Conference Ecological Truth and Environmental Research - EcoTER'22",
title = "PREPARATION OF CROSSLINKED TYRAMINE-ALGINATE HYDROGEL USING EDC/NHS WITH SELF-IMMOBILIZED HRP",
pages = "363-360",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1767"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Pantić, N., Stanković, M., Radotić, K.,& Prodanović, R.. (2022). PREPARATION OF CROSSLINKED TYRAMINE-ALGINATE HYDROGEL USING EDC/NHS WITH SELF-IMMOBILIZED HRP. in 29th International Conference Ecological Truth and Environmental Research - EcoTER'22
University of Belgrade, Technical Faculty in Bor., 360-363.
https://hdl.handle.net/21.15107/rcub_rimsi_1767

Spasojević D, Prokopijević M, Prodanović O, Pantić N, Stanković M, Radotić K, Prodanović R. PREPARATION OF CROSSLINKED TYRAMINE-ALGINATE HYDROGEL USING EDC/NHS WITH SELF-IMMOBILIZED HRP. in 29th International Conference Ecological Truth and Environmental Research - EcoTER'22. 2022;:360-363.
https://hdl.handle.net/21.15107/rcub_rimsi_1767 .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Pantić, Nevena, Stanković, Mira, Radotić, Ksenija, Prodanović, Radivoje, "PREPARATION OF CROSSLINKED TYRAMINE-ALGINATE HYDROGEL USING EDC/NHS WITH SELF-IMMOBILIZED HRP" in 29th International Conference Ecological Truth and Environmental Research - EcoTER'22 (2022):360-363,
https://hdl.handle.net/21.15107/rcub_rimsi_1767 .

TY  - CONF
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Prodanović, Olivera
AU  - Pantić, Nevena
AU  - Bartolić, Dragana
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1770
AB  - The application of enzymes for phenol removal from polluted waters is an effective and
environmentally favorable method and an ongoing worldwide research topic. Oxidoreductive
enzymes, like Soybean peroxidase (SBP), catalyze oxidation and polymerization of phenolic
compounds in the presence of H2O2. The industrial application, however, requires enzyme
immobilization on various carriers to overcome the disadvantages of using the soluble form.
Chemically modified pectin has been chosen as a carrier for entrapment of SBP inside a threedimensional
polymeric network. Immobilization of SBP was performed in an emulsion polymerization
reaction producing enzymes entrapped in covalently crosslinked tyramine-pectin in the shape of
micro-beads. The specific activity of immobilized SBP was determined using pyrogallol as a substrate.
In this study, the stability of the immobilized SBP onto modified pectin in three different molar ratios
was tested to determine the carrier with the best performance. Immobilized peroxidase has potential
for application as a biocatalyst for phenol removal from wastewater.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 29th International Conference Ecological Truth and Environmental Research
T1  - Stability of soybean peroxidase immobilized onto hydrogel micro-beads from tyramine-pectin
EP  - 353
SP  - 350
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1770
ER  - 

@conference{
author = "Prokopijević, Miloš and Spasojević, Dragica and Prodanović, Olivera and Pantić, Nevena and Bartolić, Dragana and Radotić, Ksenija and Prodanović, Radivoje",
year = "2022",
abstract = "The application of enzymes for phenol removal from polluted waters is an effective and
environmentally favorable method and an ongoing worldwide research topic. Oxidoreductive
enzymes, like Soybean peroxidase (SBP), catalyze oxidation and polymerization of phenolic
compounds in the presence of H2O2. The industrial application, however, requires enzyme
immobilization on various carriers to overcome the disadvantages of using the soluble form.
Chemically modified pectin has been chosen as a carrier for entrapment of SBP inside a threedimensional
polymeric network. Immobilization of SBP was performed in an emulsion polymerization
reaction producing enzymes entrapped in covalently crosslinked tyramine-pectin in the shape of
micro-beads. The specific activity of immobilized SBP was determined using pyrogallol as a substrate.
In this study, the stability of the immobilized SBP onto modified pectin in three different molar ratios
was tested to determine the carrier with the best performance. Immobilized peroxidase has potential
for application as a biocatalyst for phenol removal from wastewater.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "29th International Conference Ecological Truth and Environmental Research",
title = "Stability of soybean peroxidase immobilized onto hydrogel micro-beads from tyramine-pectin",
pages = "353-350",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1770"
}

Prokopijević, M., Spasojević, D., Prodanović, O., Pantić, N., Bartolić, D., Radotić, K.,& Prodanović, R.. (2022). Stability of soybean peroxidase immobilized onto hydrogel micro-beads from tyramine-pectin. in 29th International Conference Ecological Truth and Environmental Research
University of Belgrade, Technical Faculty in Bor., 350-353.
https://hdl.handle.net/21.15107/rcub_rimsi_1770

Prokopijević M, Spasojević D, Prodanović O, Pantić N, Bartolić D, Radotić K, Prodanović R. Stability of soybean peroxidase immobilized onto hydrogel micro-beads from tyramine-pectin. in 29th International Conference Ecological Truth and Environmental Research. 2022;:350-353.
https://hdl.handle.net/21.15107/rcub_rimsi_1770 .

Prokopijević, Miloš, Spasojević, Dragica, Prodanović, Olivera, Pantić, Nevena, Bartolić, Dragana, Radotić, Ksenija, Prodanović, Radivoje, "Stability of soybean peroxidase immobilized onto hydrogel micro-beads from tyramine-pectin" in 29th International Conference Ecological Truth and Environmental Research (2022):350-353,
https://hdl.handle.net/21.15107/rcub_rimsi_1770 .

TY  - CONF
AU  - Prodanović, Olivera
AU  - Pantić, Nevena
AU  - Bogdanović Pristov, Jelena
AU  - Mitrović, Aleksandra Lj.
AU  - Radotić, Ksenija
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1761
AB  - Pančićeva omorika predstavlja Balkansku endemičnu vrstu smrče i tercijarni relikt. Određen je sastav antioksidativnih enzima tokom klijanja semena omorike u fiziološkim uslovima, a radi boljeg razumevanja mehanizama otpornosti na zagađivače iz spoljašnje sredine.1 Ovo je prva studija aktivnosti enzima katalaze (CAT), superoksid dismutaze (SOD) i peroksidaze (POD) tokom klijanja dve linije semena Pančićeve omorike (A – borealis i S – srpska). Klijanje semena je praćeno tokom 7 dana. Za procenat klijavosti korišćen je proboj radikule za više od 1 milimetar kao kriterijum. Linija A je pokazala veći procenat klijavosti (74%) i veću aktivnost enzima po jedinici sveže mase klijanaca u poređenju sa linijom S (63%). CAT aktivnost kod linije A je povećana po jedinici mase klijanaca i suvih semena, a nakon 7 dana kod neisklijalih semena nije detektovana. SOD aktivnost je ostala na sličnom nivou u obe linije. Aktivnost POD na početku nije detektovana, ali se naglo povećala nakon četvrtog dana da bi sedmog bila 10 U/g sveže mase klijanaca kod linije S i 28 U/g kod A. CAT i SOD su uključeni u očuvanje klijavosti semena i imaju ulogu zaštite od reaktivnih kiseoničnih vrsta tokom skladištenja i klijanja, dok je katalazna aktivnost bitna za procenu klijavosti. Najveću promenu aktivnosti za vreme klijanja pokazala je peroksidaza, čija aktivnost nije detektovana u suvim semenima, a tokom klijanja naglo se povećala i značajna je u kasnijim fazama klijanja.
PB  - Srpsko biološko društvo
C3  - Treći kongres biologa Srbije
T1  - Klijanja semena Pančićeve omorike (Picea omorika (Pančić) Purkyně) i antioksidativni enzimi
SP  - 327
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1761
ER  - 

@conference{
author = "Prodanović, Olivera and Pantić, Nevena and Bogdanović Pristov, Jelena and Mitrović, Aleksandra Lj. and Radotić, Ksenija",
year = "2022",
abstract = "Pančićeva omorika predstavlja Balkansku endemičnu vrstu smrče i tercijarni relikt. Određen je sastav antioksidativnih enzima tokom klijanja semena omorike u fiziološkim uslovima, a radi boljeg razumevanja mehanizama otpornosti na zagađivače iz spoljašnje sredine.1 Ovo je prva studija aktivnosti enzima katalaze (CAT), superoksid dismutaze (SOD) i peroksidaze (POD) tokom klijanja dve linije semena Pančićeve omorike (A – borealis i S – srpska). Klijanje semena je praćeno tokom 7 dana. Za procenat klijavosti korišćen je proboj radikule za više od 1 milimetar kao kriterijum. Linija A je pokazala veći procenat klijavosti (74%) i veću aktivnost enzima po jedinici sveže mase klijanaca u poređenju sa linijom S (63%). CAT aktivnost kod linije A je povećana po jedinici mase klijanaca i suvih semena, a nakon 7 dana kod neisklijalih semena nije detektovana. SOD aktivnost je ostala na sličnom nivou u obe linije. Aktivnost POD na početku nije detektovana, ali se naglo povećala nakon četvrtog dana da bi sedmog bila 10 U/g sveže mase klijanaca kod linije S i 28 U/g kod A. CAT i SOD su uključeni u očuvanje klijavosti semena i imaju ulogu zaštite od reaktivnih kiseoničnih vrsta tokom skladištenja i klijanja, dok je katalazna aktivnost bitna za procenu klijavosti. Najveću promenu aktivnosti za vreme klijanja pokazala je peroksidaza, čija aktivnost nije detektovana u suvim semenima, a tokom klijanja naglo se povećala i značajna je u kasnijim fazama klijanja.",
publisher = "Srpsko biološko društvo",
journal = "Treći kongres biologa Srbije",
title = "Klijanja semena Pančićeve omorike (Picea omorika (Pančić) Purkyně) i antioksidativni enzimi",
pages = "327",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1761"
}

Prodanović, O., Pantić, N., Bogdanović Pristov, J., Mitrović, A. Lj.,& Radotić, K.. (2022). Klijanja semena Pančićeve omorike (Picea omorika (Pančić) Purkyně) i antioksidativni enzimi. in Treći kongres biologa Srbije
Srpsko biološko društvo., 327.
https://hdl.handle.net/21.15107/rcub_rimsi_1761

Prodanović O, Pantić N, Bogdanović Pristov J, Mitrović AL, Radotić K. Klijanja semena Pančićeve omorike (Picea omorika (Pančić) Purkyně) i antioksidativni enzimi. in Treći kongres biologa Srbije. 2022;:327.
https://hdl.handle.net/21.15107/rcub_rimsi_1761 .

Prodanović, Olivera, Pantić, Nevena, Bogdanović Pristov, Jelena, Mitrović, Aleksandra Lj., Radotić, Ksenija, "Klijanja semena Pančićeve omorike (Picea omorika (Pančić) Purkyně) i antioksidativni enzimi" in Treći kongres biologa Srbije (2022):327,
https://hdl.handle.net/21.15107/rcub_rimsi_1761 .

TY  - GEN
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2879
AB  - У последњих 20 година, расте интересовање за биополимере, не само међу биохемичарима и молекуларним биолозима, него и у другим научним областима, а посебно у области науке о материјалима. Главне предности биополимера у односу на полимере из фосилних горива, јесу јефтино добијање из обновљивих извора и биоразградивост. Полисахариди су најзаступљенија класа биополимера у природи. Целулоза је главна структурна компонента ћелијског зида виших биљака и по количини најобилнији биополимер на земљи. За њом следи хемицелулоза, која представља скуп хетерополисахарида различите структуре. Најзаступљенији морски полисахарид је алгинат, конституент ћелијског зида мрких морских алги. Полисахариди поседују бројне функционалне групе, погодне за различите врсте хемијских модификација. Јонизабилне групе обезбеђују им хидрофилност, као и способност везивања наелектрисаних молекула и јона. Све ове особине допринеле су да полисахариди постану одличан материјал за производњу хидрогелова. Хидрогелови на бази биополимера нашли су своју примену у индустрији, пољопривреди, фармацији, медицини, заштити животне средине...
PB  - Српско биолошко друштво, Београд
T2  - Treći kongres biologa Srbije
T1  - Biljni polisaharidi kao hidrogelovi
SP  - 281
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2879
ER  - 

@misc{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Radotić, Ksenija and Prodanović, Radivoje",
year = "2022",
abstract = "У последњих 20 година, расте интересовање за биополимере, не само међу биохемичарима и молекуларним биолозима, него и у другим научним областима, а посебно у области науке о материјалима. Главне предности биополимера у односу на полимере из фосилних горива, јесу јефтино добијање из обновљивих извора и биоразградивост. Полисахариди су најзаступљенија класа биополимера у природи. Целулоза је главна структурна компонента ћелијског зида виших биљака и по количини најобилнији биополимер на земљи. За њом следи хемицелулоза, која представља скуп хетерополисахарида различите структуре. Најзаступљенији морски полисахарид је алгинат, конституент ћелијског зида мрких морских алги. Полисахариди поседују бројне функционалне групе, погодне за различите врсте хемијских модификација. Јонизабилне групе обезбеђују им хидрофилност, као и способност везивања наелектрисаних молекула и јона. Све ове особине допринеле су да полисахариди постану одличан материјал за производњу хидрогелова. Хидрогелови на бази биополимера нашли су своју примену у индустрији, пољопривреди, фармацији, медицини, заштити животне средине...",
publisher = "Српско биолошко друштво, Београд",
journal = "Treći kongres biologa Srbije",
title = "Biljni polisaharidi kao hidrogelovi",
pages = "281",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2879"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Radotić, K.,& Prodanović, R.. (2022). Biljni polisaharidi kao hidrogelovi. in Treći kongres biologa Srbije
Српско биолошко друштво, Београд., 281.
https://hdl.handle.net/21.15107/rcub_rimsi_2879

Spasojević D, Prokopijević M, Prodanović O, Radotić K, Prodanović R. Biljni polisaharidi kao hidrogelovi. in Treći kongres biologa Srbije. 2022;:281.
https://hdl.handle.net/21.15107/rcub_rimsi_2879 .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Radotić, Ksenija, Prodanović, Radivoje, "Biljni polisaharidi kao hidrogelovi" in Treći kongres biologa Srbije (2022):281,
https://hdl.handle.net/21.15107/rcub_rimsi_2879 .

TY  - CONF
AU  - Kalicanin, Nevena
AU  - Balaz, Ana Marija
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3048
AB  - Opine dehydrogenases are a family of NAD(P)H dependent oxidoreductases, which
catalyze the reductive condensation of an α amino group from an amino acid with an αketo acid during anaerobic glycolysis by regenerating NAD. They are widespread in
cephalopods and mollusks. Opines are associated with crown gall tumor pathogenesis
caused by A. tumefaciens providing nutrients to the pathogen, and novel opine compounds
acting as metallophores have been identified. Besides, opine-type secondary amine
dicarboxylic acids are chiral intermediates of angiotensin-converting enzyme inhibitors. A
novel enzyme originating from an extremophile bacterium, with assumed opine
dehydrogenase function was successfully expressed in Escherichia coli STAR cells and
purified by affinity chromatography. Molecular mass determined by SDS-PAGE was
approximately 40 kDa. The activity was measured by using pyruvate and alanine as
substrates, by which proved that it has opine dehydrogenase activity.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry"
T1  - Production of a novel opine dehydrogenase
SP  - 79
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3048
ER  - 

@conference{
author = "Kalicanin, Nevena and Balaz, Ana Marija and Prodanović, Olivera and Prodanović, Radivoje",
year = "2022",
abstract = "Opine dehydrogenases are a family of NAD(P)H dependent oxidoreductases, which
catalyze the reductive condensation of an α amino group from an amino acid with an αketo acid during anaerobic glycolysis by regenerating NAD. They are widespread in
cephalopods and mollusks. Opines are associated with crown gall tumor pathogenesis
caused by A. tumefaciens providing nutrients to the pathogen, and novel opine compounds
acting as metallophores have been identified. Besides, opine-type secondary amine
dicarboxylic acids are chiral intermediates of angiotensin-converting enzyme inhibitors. A
novel enzyme originating from an extremophile bacterium, with assumed opine
dehydrogenase function was successfully expressed in Escherichia coli STAR cells and
purified by affinity chromatography. Molecular mass determined by SDS-PAGE was
approximately 40 kDa. The activity was measured by using pyruvate and alanine as
substrates, by which proved that it has opine dehydrogenase activity.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry"",
title = "Production of a novel opine dehydrogenase",
pages = "79",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3048"
}

Kalicanin, N., Balaz, A. M., Prodanović, O.,& Prodanović, R.. (2022). Production of a novel opine dehydrogenase. in Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry"
Faculty of Chemistry, Serbian Biochemical Society., 79.
https://hdl.handle.net/21.15107/rcub_rimsi_3048

Kalicanin N, Balaz AM, Prodanović O, Prodanović R. Production of a novel opine dehydrogenase. in Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry". 2022;:79.
https://hdl.handle.net/21.15107/rcub_rimsi_3048 .

Kalicanin, Nevena, Balaz, Ana Marija, Prodanović, Olivera, Prodanović, Radivoje, "Production of a novel opine dehydrogenase" in Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry" (2022):79,
https://hdl.handle.net/21.15107/rcub_rimsi_3048 .

TY  - JOUR
AU  - Kaličanin, Nevena
AU  - Kovačević, Gordana
AU  - Spasojević, Milica
AU  - Prodanović, Olivera
AU  - Jovanović-Šanta, Suzana
AU  - Škorić, Dušan
AU  - Opsenica, Dejan
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1768
AB  - The aim of this research was to improve the operational stability and enable the reusability of ω-transaminase for synthesis of new enantiopure chiral amines of steroids. Dihydrotestosterone was used to optimize the synthetic procedure of corresponding amino-steroid on a larger scale. The obtained product 3α-amino-5α-androstan-17β-ol was isolated and characterized. The enzyme was immobilized on a methacrylate-based carrier, giving the specific activity of 1.84 U/g of dry polymer. Higher residual activity of the immobilized enzyme in comparison to the soluble form (100 % versus 35%) after 24 h incubation in 35 % dimethylformamide (DMF) was obtained. The soluble enzyme retained 19 % of the initial activity after 2 h incubation in 35 % DMF at 70 °C, while the activity of the immobilized enzyme decreased only to 75 %. Immobilized retained 85 % of initial activity after ten consecutive cycles of 3α-amino-5α-androstan-17β-ol synthesis. We have tested the specificity of the ArRMut11 variant, further increased its stability by immobilization, and used it in several cycles for the synthesis of 3α-amino-5α-androstan-17β-ol. We showed that the enzyme previously evolved for higher stability as the immobilized variant showed more increased stability and high reusability that can more effectively be applied for the biosynthesis of amino steroids.
PB  - Elsevier
T2  - Process Biochemistry
T1  - Immobilization of ArRMut11 omega-transaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-ol
EP  - 680
SP  - 674
VL  - 121
DO  - 10.1016/j.procbio.2022.08.016
ER  - 

@article{
author = "Kaličanin, Nevena and Kovačević, Gordana and Spasojević, Milica and Prodanović, Olivera and Jovanović-Šanta, Suzana and Škorić, Dušan and Opsenica, Dejan and Prodanović, Radivoje",
year = "2022",
abstract = "The aim of this research was to improve the operational stability and enable the reusability of ω-transaminase for synthesis of new enantiopure chiral amines of steroids. Dihydrotestosterone was used to optimize the synthetic procedure of corresponding amino-steroid on a larger scale. The obtained product 3α-amino-5α-androstan-17β-ol was isolated and characterized. The enzyme was immobilized on a methacrylate-based carrier, giving the specific activity of 1.84 U/g of dry polymer. Higher residual activity of the immobilized enzyme in comparison to the soluble form (100 % versus 35%) after 24 h incubation in 35 % dimethylformamide (DMF) was obtained. The soluble enzyme retained 19 % of the initial activity after 2 h incubation in 35 % DMF at 70 °C, while the activity of the immobilized enzyme decreased only to 75 %. Immobilized retained 85 % of initial activity after ten consecutive cycles of 3α-amino-5α-androstan-17β-ol synthesis. We have tested the specificity of the ArRMut11 variant, further increased its stability by immobilization, and used it in several cycles for the synthesis of 3α-amino-5α-androstan-17β-ol. We showed that the enzyme previously evolved for higher stability as the immobilized variant showed more increased stability and high reusability that can more effectively be applied for the biosynthesis of amino steroids.",
publisher = "Elsevier",
journal = "Process Biochemistry",
title = "Immobilization of ArRMut11 omega-transaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-ol",
pages = "680-674",
volume = "121",
doi = "10.1016/j.procbio.2022.08.016"
}

Kaličanin, N., Kovačević, G., Spasojević, M., Prodanović, O., Jovanović-Šanta, S., Škorić, D., Opsenica, D.,& Prodanović, R.. (2022). Immobilization of ArRMut11 omega-transaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-ol. in Process Biochemistry
Elsevier., 121, 674-680.
https://doi.org/10.1016/j.procbio.2022.08.016

Kaličanin N, Kovačević G, Spasojević M, Prodanović O, Jovanović-Šanta S, Škorić D, Opsenica D, Prodanović R. Immobilization of ArRMut11 omega-transaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-ol. in Process Biochemistry. 2022;121:674-680.
doi:10.1016/j.procbio.2022.08.016 .

Kaličanin, Nevena, Kovačević, Gordana, Spasojević, Milica, Prodanović, Olivera, Jovanović-Šanta, Suzana, Škorić, Dušan, Opsenica, Dejan, Prodanović, Radivoje, "Immobilization of ArRMut11 omega-transaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-ol" in Process Biochemistry, 121 (2022):674-680,
https://doi.org/10.1016/j.procbio.2022.08.016 . .

TY  - JOUR
AU  - Kovačević, G.
AU  - Elgahwash, R.G.A.
AU  - Blažić, M.
AU  - Pantić, Nevena
AU  - Prodanović, Olivera
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1543
AB  - Saccharomyces cerevisiae, known as bakers’ yeast, is one of the most utilized yeasts in industry. Several enzymes that are naturally produced by yeast, such as invertase and catalase, combined with heterologously expressed glucose oxidase (GOx), represent the enzyme machinery for fructose and gluconic acid production. Therefore, we have used yeast cell walls with expressed glucose oxidase as a platform for crosslinking with invertase and catalase to create biocatalyst cells for the high yield sucrose conversion. Using 5% (w/v) suspension of cross-linked yeast cell walls in 0.15 M sucrose solution, 1.86 g L−1 h−1 of gluconic acid has been obtained using wt-GOx, while mutant A2-GOx produced 2.91 g L−1 h−1 of gluconic acid. Increasing the concentration of modified yeast cells walls to 10% (w/v) we were able to obtain almost 100% conversion of glucose to gluconic acid using A2-GOx in the first cycle. Reusing the modified cells walls in three consecutive cycles, conversion dropped to approximately 70% using A2-GOx and 40% using wt-GOx.
PB  - Elsevier B.V.
T2  - Molecular Catalysis
T1  - Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface
VL  - 522
DO  - 10.1016/j.mcat.2022.112215
ER  - 

@article{
author = "Kovačević, G. and Elgahwash, R.G.A. and Blažić, M. and Pantić, Nevena and Prodanović, Olivera and Balaž, Ana Marija and Prodanović, Radivoje",
year = "2022",
abstract = "Saccharomyces cerevisiae, known as bakers’ yeast, is one of the most utilized yeasts in industry. Several enzymes that are naturally produced by yeast, such as invertase and catalase, combined with heterologously expressed glucose oxidase (GOx), represent the enzyme machinery for fructose and gluconic acid production. Therefore, we have used yeast cell walls with expressed glucose oxidase as a platform for crosslinking with invertase and catalase to create biocatalyst cells for the high yield sucrose conversion. Using 5% (w/v) suspension of cross-linked yeast cell walls in 0.15 M sucrose solution, 1.86 g L−1 h−1 of gluconic acid has been obtained using wt-GOx, while mutant A2-GOx produced 2.91 g L−1 h−1 of gluconic acid. Increasing the concentration of modified yeast cells walls to 10% (w/v) we were able to obtain almost 100% conversion of glucose to gluconic acid using A2-GOx in the first cycle. Reusing the modified cells walls in three consecutive cycles, conversion dropped to approximately 70% using A2-GOx and 40% using wt-GOx.",
publisher = "Elsevier B.V.",
journal = "Molecular Catalysis",
title = "Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface",
volume = "522",
doi = "10.1016/j.mcat.2022.112215"
}

Kovačević, G., Elgahwash, R.G.A., Blažić, M., Pantić, N., Prodanović, O., Balaž, A. M.,& Prodanović, R.. (2022). Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface. in Molecular Catalysis
Elsevier B.V.., 522.
https://doi.org/10.1016/j.mcat.2022.112215

Kovačević G, Elgahwash R, Blažić M, Pantić N, Prodanović O, Balaž AM, Prodanović R. Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface. in Molecular Catalysis. 2022;522.
doi:10.1016/j.mcat.2022.112215 .

Kovačević, G., Elgahwash, R.G.A., Blažić, M., Pantić, Nevena, Prodanović, Olivera, Balaž, Ana Marija, Prodanović, Radivoje, "Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface" in Molecular Catalysis, 522 (2022),
https://doi.org/10.1016/j.mcat.2022.112215 . .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Spasojević, Milica
AU  - Stojanović, Zeljko P
AU  - Veljović, Đorđe
AU  - Krstic, Jugoslav
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1530
AB  - Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA-co-EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 degrees C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased K-m value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.
PB  - Springer, New York
T2  - Journal of Polymers and the Environment
T1  - Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol
DO  - 10.1007/s10924-021-02364-3
ER  - 

@article{
author = "Pantić, Nevena and Spasojević, Milica and Stojanović, Zeljko P and Veljović, Đorđe and Krstic, Jugoslav and Balaž, Ana Marija and Prodanović, Radivoje and Prodanović, Olivera",
year = "2022",
abstract = "Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA-co-EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 degrees C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased K-m value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.",
publisher = "Springer, New York",
journal = "Journal of Polymers and the Environment",
title = "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol",
doi = "10.1007/s10924-021-02364-3"
}

Pantić, N., Spasojević, M., Stojanović, Z. P., Veljović, Đ., Krstic, J., Balaž, A. M., Prodanović, R.,& Prodanović, O.. (2022). Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment
Springer, New York..
https://doi.org/10.1007/s10924-021-02364-3

Pantić N, Spasojević M, Stojanović ZP, Veljović Đ, Krstic J, Balaž AM, Prodanović R, Prodanović O. Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment. 2022;.
doi:10.1007/s10924-021-02364-3 .

Pantić, Nevena, Spasojević, Milica, Stojanović, Zeljko P, Veljović, Đorđe, Krstic, Jugoslav, Balaž, Ana Marija, Prodanović, Radivoje, Prodanović, Olivera, "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol" in Journal of Polymers and the Environment (2022),
https://doi.org/10.1007/s10924-021-02364-3 . .

TY  - CONF
AU  - Spasojević, Dragica
AU  - Stanković, Mira
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Stojkovska, Jasmina
AU  - Obradović, Bojana
AU  - Radotić, Ksenija
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1759
AB  - INTRODUCTION:
Alginate dressings are widely used in the treatment of exuding wounds29. The enzymatically synthesized lignin model compound dehydrogenate polymer (DHP) from coniferyl alcohol by the enzyme peroxidase, is the best lignin substitute used in
various experiments30. In our previous work, we have shown that synthesized DHP has antibacterial and antibiofilm properties, and in combination with alginate has good potential for wound treatment31.
OBJECTIVES:
The objective of this paper was to study the sustained release of DHP from low and medium viscosity alginate beads.
PB  - Prirodno-matematički fakultet Novi Sad
C3  - International Bioscience Conference and the 8th International PSU – UNS Bioscience Conference IBSC2021
T1  - Sustained release of lignin model compound dehydrogenate polymer (DHP) from alginate beads
EP  - 133
SP  - 132
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1759
ER  - 

@conference{
author = "Spasojević, Dragica and Stanković, Mira and Prokopijević, Miloš and Prodanović, Olivera and Stojkovska, Jasmina and Obradović, Bojana and Radotić, Ksenija",
year = "2021",
abstract = "INTRODUCTION:
Alginate dressings are widely used in the treatment of exuding wounds29. The enzymatically synthesized lignin model compound dehydrogenate polymer (DHP) from coniferyl alcohol by the enzyme peroxidase, is the best lignin substitute used in
various experiments30. In our previous work, we have shown that synthesized DHP has antibacterial and antibiofilm properties, and in combination with alginate has good potential for wound treatment31.
OBJECTIVES:
The objective of this paper was to study the sustained release of DHP from low and medium viscosity alginate beads.",
publisher = "Prirodno-matematički fakultet Novi Sad",
journal = "International Bioscience Conference and the 8th International PSU – UNS Bioscience Conference IBSC2021",
title = "Sustained release of lignin model compound dehydrogenate polymer (DHP) from alginate beads",
pages = "133-132",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1759"
}

Spasojević, D., Stanković, M., Prokopijević, M., Prodanović, O., Stojkovska, J., Obradović, B.,& Radotić, K.. (2021). Sustained release of lignin model compound dehydrogenate polymer (DHP) from alginate beads. in International Bioscience Conference and the 8th International PSU – UNS Bioscience Conference IBSC2021
Prirodno-matematički fakultet Novi Sad., 132-133.
https://hdl.handle.net/21.15107/rcub_rimsi_1759

Spasojević D, Stanković M, Prokopijević M, Prodanović O, Stojkovska J, Obradović B, Radotić K. Sustained release of lignin model compound dehydrogenate polymer (DHP) from alginate beads. in International Bioscience Conference and the 8th International PSU – UNS Bioscience Conference IBSC2021. 2021;:132-133.
https://hdl.handle.net/21.15107/rcub_rimsi_1759 .

Spasojević, Dragica, Stanković, Mira, Prokopijević, Miloš, Prodanović, Olivera, Stojkovska, Jasmina, Obradović, Bojana, Radotić, Ksenija, "Sustained release of lignin model compound dehydrogenate polymer (DHP) from alginate beads" in International Bioscience Conference and the 8th International PSU – UNS Bioscience Conference IBSC2021 (2021):132-133,
https://hdl.handle.net/21.15107/rcub_rimsi_1759 .

TY  - CONF
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Pantić, Nevena
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1790
AB  - Hemicellulose rich in xylan was isolated from corncobs. Functional groups were introduced first by
carboxymethylation and then by coupling with tyramine via carbodiimide-mediated reaction.
Obtained hydrogel was tested for horseradish peroxidase (HRP) immobilization within microbeads,
formed in an emulsion based enzymatic polymerization reaction. This model system showed that
modified hemicellulose isolated from corncob is a suitable candidate for enzyme or small molecule
immobilization for different purposes.
PB  - Society of Physical Chemists of Serbia
C3  - 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry
T1  - Chemical modification of hemicellulose isolated from corncobs to obtain hydrogel for enzyme immobilization
EP  - 342
SP  - 340
VL  - 1
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1790
ER  - 

@conference{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Pantić, Nevena and Radotić, Ksenija and Prodanović, Radivoje",
year = "2021",
abstract = "Hemicellulose rich in xylan was isolated from corncobs. Functional groups were introduced first by
carboxymethylation and then by coupling with tyramine via carbodiimide-mediated reaction.
Obtained hydrogel was tested for horseradish peroxidase (HRP) immobilization within microbeads,
formed in an emulsion based enzymatic polymerization reaction. This model system showed that
modified hemicellulose isolated from corncob is a suitable candidate for enzyme or small molecule
immobilization for different purposes.",
publisher = "Society of Physical Chemists of Serbia",
journal = "15th International Conference on Fundamental and Applied Aspects of Physical Chemistry",
title = "Chemical modification of hemicellulose isolated from corncobs to obtain hydrogel for enzyme immobilization",
pages = "342-340",
volume = "1",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1790"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Pantić, N., Radotić, K.,& Prodanović, R.. (2021). Chemical modification of hemicellulose isolated from corncobs to obtain hydrogel for enzyme immobilization. in 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry
Society of Physical Chemists of Serbia., 1, 340-342.
https://hdl.handle.net/21.15107/rcub_rimsi_1790

Spasojević D, Prokopijević M, Prodanović O, Pantić N, Radotić K, Prodanović R. Chemical modification of hemicellulose isolated from corncobs to obtain hydrogel for enzyme immobilization. in 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry. 2021;1:340-342.
https://hdl.handle.net/21.15107/rcub_rimsi_1790 .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Pantić, Nevena, Radotić, Ksenija, Prodanović, Radivoje, "Chemical modification of hemicellulose isolated from corncobs to obtain hydrogel for enzyme immobilization" in 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry, 1 (2021):340-342,
https://hdl.handle.net/21.15107/rcub_rimsi_1790 .

TY  - JOUR
AU  - Mitrović, Aleksandra Lj.
AU  - Simonović Radosavljević, Jasna
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Kovacević, Jovana
AU  - Prodanović, Olivera
AU  - Todorović, Bratislav
AU  - Matović, Branko
AU  - Stanković, Mira
AU  - Maksimović, Vuk
AU  - Mutavdžić, Dragosav
AU  - Skocic, Milos
AU  - Pesic, Mirjana
AU  - Prokic, Ljiljana
AU  - Radotić, Ksenija
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1449
AB  - The UV-B represents the minor fraction of the solar spectrum, while UV-C is not contained in natural solar radiation, but both radiation types can cause damaging effects in plants. Cell walls (CWs) are one of the targets for external stressors. Juvenile P. omorika trees were treated either with 21 day-high doses UV-B or with 7 day-UV-C in open-top chambers. Using spectroscopic and biochemical techniques, it was shown that the response to UV radiation includes numerous modifications in needle CW structure: relative content of xylan, xyloglucan, lignin and cellulose decreased; cellulose crystallinity changed; yield of lignin monomers with stronger connection of C=C in side chain with the ring increased; re-distribution of inter- and intra-polymer H-bonds occurred. The recovery was mediated by an increase in the activities and changes in isoform profiles of CW bound covalent peroxidases (POD) and polyphenol oxidases (PO) (UV-B), and ionic POD and covalent PO (UV-C). A connection between activities of specific POD/PO isoforms and phenolic species (m- and p-coumaric acid, pinoresinol and cinnamic acid derivatives) was demonstrated, and supported by changes in the sRNA profile. In vivo fluorometry showed phenolics accumulation in needle epidermal CWs. These results imply transversal connections between polymers and changed mechanical properties of needle CW as a response to UV. The CW alterations enabled maintenance of physiological functions, as indicated by the preserved chlorophyll content and/or organization. The current study provides evidence that in conifers, needle CW response to both UV-B and UV-C includes biochemical modifications and structural remodeling.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux
T2  - Plant Physiology and Biochemistry
T1  - Cell wall response to UV radiation in needles of Picea omorika
EP  - 190
SP  - 176
VL  - 161
DO  - 10.1016/j.plaphy.2021.02.007
ER  - 

@article{
author = "Mitrović, Aleksandra Lj. and Simonović Radosavljević, Jasna and Prokopijević, Miloš and Spasojević, Dragica and Kovacević, Jovana and Prodanović, Olivera and Todorović, Bratislav and Matović, Branko and Stanković, Mira and Maksimović, Vuk and Mutavdžić, Dragosav and Skocic, Milos and Pesic, Mirjana and Prokic, Ljiljana and Radotić, Ksenija",
year = "2021",
abstract = "The UV-B represents the minor fraction of the solar spectrum, while UV-C is not contained in natural solar radiation, but both radiation types can cause damaging effects in plants. Cell walls (CWs) are one of the targets for external stressors. Juvenile P. omorika trees were treated either with 21 day-high doses UV-B or with 7 day-UV-C in open-top chambers. Using spectroscopic and biochemical techniques, it was shown that the response to UV radiation includes numerous modifications in needle CW structure: relative content of xylan, xyloglucan, lignin and cellulose decreased; cellulose crystallinity changed; yield of lignin monomers with stronger connection of C=C in side chain with the ring increased; re-distribution of inter- and intra-polymer H-bonds occurred. The recovery was mediated by an increase in the activities and changes in isoform profiles of CW bound covalent peroxidases (POD) and polyphenol oxidases (PO) (UV-B), and ionic POD and covalent PO (UV-C). A connection between activities of specific POD/PO isoforms and phenolic species (m- and p-coumaric acid, pinoresinol and cinnamic acid derivatives) was demonstrated, and supported by changes in the sRNA profile. In vivo fluorometry showed phenolics accumulation in needle epidermal CWs. These results imply transversal connections between polymers and changed mechanical properties of needle CW as a response to UV. The CW alterations enabled maintenance of physiological functions, as indicated by the preserved chlorophyll content and/or organization. The current study provides evidence that in conifers, needle CW response to both UV-B and UV-C includes biochemical modifications and structural remodeling.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux",
journal = "Plant Physiology and Biochemistry",
title = "Cell wall response to UV radiation in needles of Picea omorika",
pages = "190-176",
volume = "161",
doi = "10.1016/j.plaphy.2021.02.007"
}

Mitrović, A. Lj., Simonović Radosavljević, J., Prokopijević, M., Spasojević, D., Kovacević, J., Prodanović, O., Todorović, B., Matović, B., Stanković, M., Maksimović, V., Mutavdžić, D., Skocic, M., Pesic, M., Prokic, L.,& Radotić, K.. (2021). Cell wall response to UV radiation in needles of Picea omorika. in Plant Physiology and Biochemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux., 161, 176-190.
https://doi.org/10.1016/j.plaphy.2021.02.007

Mitrović AL, Simonović Radosavljević J, Prokopijević M, Spasojević D, Kovacević J, Prodanović O, Todorović B, Matović B, Stanković M, Maksimović V, Mutavdžić D, Skocic M, Pesic M, Prokic L, Radotić K. Cell wall response to UV radiation in needles of Picea omorika. in Plant Physiology and Biochemistry. 2021;161:176-190.
doi:10.1016/j.plaphy.2021.02.007 .

Mitrović, Aleksandra Lj., Simonović Radosavljević, Jasna, Prokopijević, Miloš, Spasojević, Dragica, Kovacević, Jovana, Prodanović, Olivera, Todorović, Bratislav, Matović, Branko, Stanković, Mira, Maksimović, Vuk, Mutavdžić, Dragosav, Skocic, Milos, Pesic, Mirjana, Prokic, Ljiljana, Radotić, Ksenija, "Cell wall response to UV radiation in needles of Picea omorika" in Plant Physiology and Biochemistry, 161 (2021):176-190,
https://doi.org/10.1016/j.plaphy.2021.02.007 . .

TY  - JOUR
AU  - Popović, Nikolina
AU  - Przulj, Dunja
AU  - Mladenović, Maja
AU  - Prodanović, Olivera
AU  - Ece, Selin
AU  - Ilic-Durdic, Karla
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1490
AB  - High amounts of toxic textile dyes are released into the environment due to coloring and wastewaters treatment processes' inefficiency. To remove dyes from the environment and wastewaters, researchers focused on applying immobilized enzymes due to mild reaction conditions and enzyme nontoxicity. Laccases are oxidases with wide substrate specificity, capable of degradation of many different dye types. Laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The specific activity of surface-displayed laccase was increased by toluene-induced lysis to 3.1 U/g of cell walls. For cell wall laccase immobilization within hydrogel beads, alginate was modified by dopamine using periodate oxidation and reductive amination and characterized by UV-Vis, FTIR, and NMR spectroscopy. Cell wall laccase was immobilized within alginate and dopamine-alginate beads additionally cross-linked by oxygen and laccase. The immobilized enzyme's specific activity was two times higher using dopamine-alginate compared to native alginate beads, and immobilization yield increased 16 times. Cell wall laccase immobilized within dopamine-alginate beads decolorized Amido Black 10B, Reactive Black 5, Evans Blue, and Remazol Brilliant Blue with 100% efficiency and after ten rounds of multiple-use retained decolorization efficiency of 90% with Evans Blue and 61% with Amido Black.
PB  - Elsevier, Amsterdam
T2  - International Journal of Biological Macromolecules
T1  - Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization
EP  - 1080
SP  - 1072
VL  - 181
DO  - 10.1016/j.ijbiomac.2021.04.115
ER  - 

@article{
author = "Popović, Nikolina and Przulj, Dunja and Mladenović, Maja and Prodanović, Olivera and Ece, Selin and Ilic-Durdic, Karla and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2021",
abstract = "High amounts of toxic textile dyes are released into the environment due to coloring and wastewaters treatment processes' inefficiency. To remove dyes from the environment and wastewaters, researchers focused on applying immobilized enzymes due to mild reaction conditions and enzyme nontoxicity. Laccases are oxidases with wide substrate specificity, capable of degradation of many different dye types. Laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The specific activity of surface-displayed laccase was increased by toluene-induced lysis to 3.1 U/g of cell walls. For cell wall laccase immobilization within hydrogel beads, alginate was modified by dopamine using periodate oxidation and reductive amination and characterized by UV-Vis, FTIR, and NMR spectroscopy. Cell wall laccase was immobilized within alginate and dopamine-alginate beads additionally cross-linked by oxygen and laccase. The immobilized enzyme's specific activity was two times higher using dopamine-alginate compared to native alginate beads, and immobilization yield increased 16 times. Cell wall laccase immobilized within dopamine-alginate beads decolorized Amido Black 10B, Reactive Black 5, Evans Blue, and Remazol Brilliant Blue with 100% efficiency and after ten rounds of multiple-use retained decolorization efficiency of 90% with Evans Blue and 61% with Amido Black.",
publisher = "Elsevier, Amsterdam",
journal = "International Journal of Biological Macromolecules",
title = "Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization",
pages = "1080-1072",
volume = "181",
doi = "10.1016/j.ijbiomac.2021.04.115"
}

Popović, N., Przulj, D., Mladenović, M., Prodanović, O., Ece, S., Ilic-Durdic, K., Ostafe, R., Fischer, R.,& Prodanović, R.. (2021). Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization. in International Journal of Biological Macromolecules
Elsevier, Amsterdam., 181, 1072-1080.
https://doi.org/10.1016/j.ijbiomac.2021.04.115

Popović N, Przulj D, Mladenović M, Prodanović O, Ece S, Ilic-Durdic K, Ostafe R, Fischer R, Prodanović R. Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization. in International Journal of Biological Macromolecules. 2021;181:1072-1080.
doi:10.1016/j.ijbiomac.2021.04.115 .

Popović, Nikolina, Przulj, Dunja, Mladenović, Maja, Prodanović, Olivera, Ece, Selin, Ilic-Durdic, Karla, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization" in International Journal of Biological Macromolecules, 181 (2021):1072-1080,
https://doi.org/10.1016/j.ijbiomac.2021.04.115 . .

TY  - JOUR
AU  - Ilic-Durdic, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Durdevic-Delmas, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1488
AB  - The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) fromPhanerochaete chrysosporiumis a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 10(4) independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.
PB  - Higher Education Press, Beijing
T2  - Frontiers of Environmental Science & Engineering
T1  - Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls
IS  - 2
VL  - 15
DO  - 10.1007/s11783-020-1311-4
ER  - 

@article{
author = "Ilic-Durdic, Karla and Ostafe, Raluca and Prodanović, Olivera and Durdevic-Delmas, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
abstract = "The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) fromPhanerochaete chrysosporiumis a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 10(4) independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.",
publisher = "Higher Education Press, Beijing",
journal = "Frontiers of Environmental Science & Engineering",
title = "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls",
number = "2",
volume = "15",
doi = "10.1007/s11783-020-1311-4"
}

Ilic-Durdic, K., Ostafe, R., Prodanović, O., Durdevic-Delmas, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering
Higher Education Press, Beijing., 15(2).
https://doi.org/10.1007/s11783-020-1311-4

Ilic-Durdic K, Ostafe R, Prodanović O, Durdevic-Delmas A, Popović N, Fischer R, Schillberg S, Prodanović R. Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering. 2021;15(2).
doi:10.1007/s11783-020-1311-4 .

Ilic-Durdic, Karla, Ostafe, Raluca, Prodanović, Olivera, Durdevic-Delmas, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls" in Frontiers of Environmental Science & Engineering, 15, no. 2 (2021),
https://doi.org/10.1007/s11783-020-1311-4 . .

TY  - JOUR
AU  - Popović, Nikolina
AU  - Stanisic, Marija
AU  - Ilic-Durdic, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1484
AB  - Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV-Vis, FTIR, and H-1 NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.
PB  - Elsevier, Amsterdam
T2  - Environmental Technology & Innovation
T1  - Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization
VL  - 22
DO  - 10.1016/j.eti.2021.101399
ER  - 

@article{
author = "Popović, Nikolina and Stanisic, Marija and Ilic-Durdic, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
abstract = "Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV-Vis, FTIR, and H-1 NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.",
publisher = "Elsevier, Amsterdam",
journal = "Environmental Technology & Innovation",
title = "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization",
volume = "22",
doi = "10.1016/j.eti.2021.101399"
}

Popović, N., Stanisic, M., Ilic-Durdic, K., Prodanović, O., Polović, N.,& Prodanović, R.. (2021). Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. in Environmental Technology & Innovation
Elsevier, Amsterdam., 22.
https://doi.org/10.1016/j.eti.2021.101399

Popović N, Stanisic M, Ilic-Durdic K, Prodanović O, Polović N, Prodanović R. Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. in Environmental Technology & Innovation. 2021;22.
doi:10.1016/j.eti.2021.101399 .

Popović, Nikolina, Stanisic, Marija, Ilic-Durdic, Karla, Prodanović, Olivera, Polović, Natalija, Prodanović, Radivoje, "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization" in Environmental Technology & Innovation, 22 (2021),
https://doi.org/10.1016/j.eti.2021.101399 . .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Prodanović, Radivoje
AU  - Ilic-Durdic, Karla
AU  - Polović, Natalija
AU  - Spasojević, Milica
AU  - Prodanović, Olivera
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1476
AB  - Removal of phenolic compounds from water is of major interest over the years, since they are one of the most common pollutants in aqueous systems. Horseradish peroxidase (HRP) is the most investigated biocatalyst for this purpose. Inactivation of the enzyme is a major issue which can be successfully overcome by the enzyme immobilization on different polymers. In this study, tyramine-alginate micro-beads were used as carriers for the immobilization of horseradish peroxidase. The effect of the oxidation degree of tyramine-alginates on a specific activity of the enzyme was tested. An increase in the concentration of oxidized alginate from 2.5 to 20% resulted in a gradual increase in the specific activity from 0.05 to 0.67 U/mL. HRP immobilized within these microbeads was tested for the phenol removal in a batch reactor. Reaction conditions were optimized to achieve a high removal efficiency and substantial reusability of the system. In this study, for the first time, an internal generation of hydrogen peroxide from glucose and glucose oxidase was employed in the phenol removal process with HRP immobilized on tyramine-alginate. Within 6 h of repeated use 96% of phenol was removed when the system for internal delivery of H2O2, composed of 0.187 U/mL of glucose oxidase and 4 mmol/L of glucose was employed. A common straightforward addition of hydrogen peroxide provided the removal efficiency of only 42%, under the same reaction conditions. The highest efficiency of the phenol removal (96%) was obtained with HRP immobilized within 20 mol% oxidized tyramine-alginate microbeads. Fifteen mol% oxidized tyramine-alginate showed lower removal efficiency in the first cycle of use (73%) but more promising reusability, since the immobilized enzyme retained 61% of its initial activity even after four consecutive cycles of use.
PB  - Elsevier, Amsterdam
T2  - Environmental Technology & Innovation
T1  - Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads
VL  - 21
DO  - 10.1016/j.eti.2020.101211
ER  - 

@article{
author = "Pantić, Nevena and Prodanović, Radivoje and Ilic-Durdic, Karla and Polović, Natalija and Spasojević, Milica and Prodanović, Olivera",
year = "2021",
abstract = "Removal of phenolic compounds from water is of major interest over the years, since they are one of the most common pollutants in aqueous systems. Horseradish peroxidase (HRP) is the most investigated biocatalyst for this purpose. Inactivation of the enzyme is a major issue which can be successfully overcome by the enzyme immobilization on different polymers. In this study, tyramine-alginate micro-beads were used as carriers for the immobilization of horseradish peroxidase. The effect of the oxidation degree of tyramine-alginates on a specific activity of the enzyme was tested. An increase in the concentration of oxidized alginate from 2.5 to 20% resulted in a gradual increase in the specific activity from 0.05 to 0.67 U/mL. HRP immobilized within these microbeads was tested for the phenol removal in a batch reactor. Reaction conditions were optimized to achieve a high removal efficiency and substantial reusability of the system. In this study, for the first time, an internal generation of hydrogen peroxide from glucose and glucose oxidase was employed in the phenol removal process with HRP immobilized on tyramine-alginate. Within 6 h of repeated use 96% of phenol was removed when the system for internal delivery of H2O2, composed of 0.187 U/mL of glucose oxidase and 4 mmol/L of glucose was employed. A common straightforward addition of hydrogen peroxide provided the removal efficiency of only 42%, under the same reaction conditions. The highest efficiency of the phenol removal (96%) was obtained with HRP immobilized within 20 mol% oxidized tyramine-alginate microbeads. Fifteen mol% oxidized tyramine-alginate showed lower removal efficiency in the first cycle of use (73%) but more promising reusability, since the immobilized enzyme retained 61% of its initial activity even after four consecutive cycles of use.",
publisher = "Elsevier, Amsterdam",
journal = "Environmental Technology & Innovation",
title = "Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads",
volume = "21",
doi = "10.1016/j.eti.2020.101211"
}

Pantić, N., Prodanović, R., Ilic-Durdic, K., Polović, N., Spasojević, M.,& Prodanović, O.. (2021). Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads. in Environmental Technology & Innovation
Elsevier, Amsterdam., 21.
https://doi.org/10.1016/j.eti.2020.101211

Pantić N, Prodanović R, Ilic-Durdic K, Polović N, Spasojević M, Prodanović O. Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads. in Environmental Technology & Innovation. 2021;21.
doi:10.1016/j.eti.2020.101211 .

Pantić, Nevena, Prodanović, Radivoje, Ilic-Durdic, Karla, Polović, Natalija, Spasojević, Milica, Prodanović, Olivera, "Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads" in Environmental Technology & Innovation, 21 (2021),
https://doi.org/10.1016/j.eti.2020.101211 . .

TY  - JOUR
AU  - Balaž, Ana Marija
AU  - BLazic, Marija B.
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1297
AB  - Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZ alpha plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion-exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s(-1) for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM(-1) s(-1). All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain
EP  - 35
IS  - 1
SP  - 25
VL  - 85
DO  - 10.2298/JSC190320058B
ER  - 

@article{
author = "Balaž, Ana Marija and BLazic, Marija B. and Popović, Nikolina and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZ alpha plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion-exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s(-1) for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM(-1) s(-1). All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain",
pages = "35-25",
number = "1",
volume = "85",
doi = "10.2298/JSC190320058B"
}

Balaž, A. M., BLazic, M. B., Popović, N., Prodanović, O., Ostafe, R., Fischer, R.,& Prodanović, R.. (2020). Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 85(1), 25-35.
https://doi.org/10.2298/JSC190320058B

Balaž AM, BLazic MB, Popović N, Prodanović O, Ostafe R, Fischer R, Prodanović R. Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society. 2020;85(1):25-35.
doi:10.2298/JSC190320058B .

Balaž, Ana Marija, BLazic, Marija B., Popović, Nikolina, Prodanović, Olivera, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain" in Journal of the Serbian Chemical Society, 85, no. 1 (2020):25-35,
https://doi.org/10.2298/JSC190320058B . .

TY  - CONF
AU  - Pantić, Nevena
AU  - Popović, Nikolina
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Prodanović, Radivoje
AU  - Đikanović, Daniela
AU  - Prodanović, Olivera
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1656
AB  - Phenolic compounds are one of the most common pollutants in aqueous systems, so their removal
from water is of major interest. Among biocatalysts used for phenol removal, horseradish peroxidase
is the most investigated for this purpose. Enzyme inactivation is a major problem which could be
successfully overcome by immobilization of the enzyme onto different polymers. Tyramine-alginate
micro-beads were tested for the immobilization of horseradish peroxidase. Different concentrations of
tyramine-alginate were used and their influence on specific activity of the enzyme was tested.
Increasing concentration of oxidized alginate results in increase of specific activity. Immobilized HRP
was tested for phenol removal in a batch reactor. Presented results were obtained with HRP
immobilized within 10 mol% tyramine-alginate micro-beads. These biocatalysts can be used up to
three cycles.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 27th International Conference Ecological Truth and Environmental Research
T1  - OPTIMIZATION OF HORSERADISH PEROXIDASE ENCAPSULATION WITHIN TYRAMINE-ALGINATE FOR PHENOL REMOVAL
SP  - 220-223
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1656
ER  - 

@conference{
author = "Pantić, Nevena and Popović, Nikolina and Prokopijević, Miloš and Spasojević, Dragica and Prodanović, Radivoje and Đikanović, Daniela and Prodanović, Olivera",
year = "2019",
abstract = "Phenolic compounds are one of the most common pollutants in aqueous systems, so their removal
from water is of major interest. Among biocatalysts used for phenol removal, horseradish peroxidase
is the most investigated for this purpose. Enzyme inactivation is a major problem which could be
successfully overcome by immobilization of the enzyme onto different polymers. Tyramine-alginate
micro-beads were tested for the immobilization of horseradish peroxidase. Different concentrations of
tyramine-alginate were used and their influence on specific activity of the enzyme was tested.
Increasing concentration of oxidized alginate results in increase of specific activity. Immobilized HRP
was tested for phenol removal in a batch reactor. Presented results were obtained with HRP
immobilized within 10 mol% tyramine-alginate micro-beads. These biocatalysts can be used up to
three cycles.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "27th International Conference Ecological Truth and Environmental Research",
title = "OPTIMIZATION OF HORSERADISH PEROXIDASE ENCAPSULATION WITHIN TYRAMINE-ALGINATE FOR PHENOL REMOVAL",
pages = "220-223",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1656"
}

Pantić, N., Popović, N., Prokopijević, M., Spasojević, D., Prodanović, R., Đikanović, D.,& Prodanović, O.. (2019). OPTIMIZATION OF HORSERADISH PEROXIDASE ENCAPSULATION WITHIN TYRAMINE-ALGINATE FOR PHENOL REMOVAL. in 27th International Conference Ecological Truth and Environmental Research
University of Belgrade, Technical Faculty in Bor., 220-223.
https://hdl.handle.net/21.15107/rcub_rimsi_1656

Pantić N, Popović N, Prokopijević M, Spasojević D, Prodanović R, Đikanović D, Prodanović O. OPTIMIZATION OF HORSERADISH PEROXIDASE ENCAPSULATION WITHIN TYRAMINE-ALGINATE FOR PHENOL REMOVAL. in 27th International Conference Ecological Truth and Environmental Research. 2019;:220-223.
https://hdl.handle.net/21.15107/rcub_rimsi_1656 .

Pantić, Nevena, Popović, Nikolina, Prokopijević, Miloš, Spasojević, Dragica, Prodanović, Radivoje, Đikanović, Daniela, Prodanović, Olivera, "OPTIMIZATION OF HORSERADISH PEROXIDASE ENCAPSULATION WITHIN TYRAMINE-ALGINATE FOR PHENOL REMOVAL" in 27th International Conference Ecological Truth and Environmental Research (2019):220-223,
https://hdl.handle.net/21.15107/rcub_rimsi_1656 .

TY  - CONF
AU  - Prokopijević, Miloš
AU  - Pantić, Nevena
AU  - Spasojević, Dragica
AU  - Prodanović, Olivera
AU  - Simonović Radosavljević, Jasna
AU  - Đikanović, Daniela
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1657
AB  - Horseradish peroxidase (HRP, E.C. 1.11.1.7) catalyzes oxidation of aqueous aromatic compounds
using hydrogen peroxide. Enzymatic treatment methods for phenol removal from wastewaters has
become an efficient and environmentally friendly alternative for the traditional methods.
Carboxymethyl cellulose (CMC) derivative with tyramine attached via amide bond to carboxyl groups
has been chosen as carrier for immobilization. In effort to overcome the main disadvantage of
entrapment immobilization method, loss of enzyme activity due to washing out from the carrier, HRP
was modified in a reductive amination reaction and tyramine was bound to the enzyme.
Immobilization of tyramine-HRP onto tyramide-carboxymethyl cellulose carrier was carried in an
emulsion polymerization reaction that produced carboxymethyl cellulose microbeads. The highest
specific activity of the obtained biocatalyst was 0.227 U/ml and after 48h of storage 0.197 U/ml.
Immobilized tyramine-HRP retained 87% of activity after 48 h. Immobilized HRP is a suitable
candidate for wastewater treatment.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 27th International Conference Ecological Truth and Environmental Research
T1  - IMMOBILIZATION OF TYRAMINE-HRP ONTO TYRAMIDECARBOXYMETHYL CELLULOSE MATRIX FOR WASTEWATER TREATMENT
SP  - 224-227
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1657
ER  - 

@conference{
author = "Prokopijević, Miloš and Pantić, Nevena and Spasojević, Dragica and Prodanović, Olivera and Simonović Radosavljević, Jasna and Đikanović, Daniela and Prodanović, Radivoje",
year = "2019",
abstract = "Horseradish peroxidase (HRP, E.C. 1.11.1.7) catalyzes oxidation of aqueous aromatic compounds
using hydrogen peroxide. Enzymatic treatment methods for phenol removal from wastewaters has
become an efficient and environmentally friendly alternative for the traditional methods.
Carboxymethyl cellulose (CMC) derivative with tyramine attached via amide bond to carboxyl groups
has been chosen as carrier for immobilization. In effort to overcome the main disadvantage of
entrapment immobilization method, loss of enzyme activity due to washing out from the carrier, HRP
was modified in a reductive amination reaction and tyramine was bound to the enzyme.
Immobilization of tyramine-HRP onto tyramide-carboxymethyl cellulose carrier was carried in an
emulsion polymerization reaction that produced carboxymethyl cellulose microbeads. The highest
specific activity of the obtained biocatalyst was 0.227 U/ml and after 48h of storage 0.197 U/ml.
Immobilized tyramine-HRP retained 87% of activity after 48 h. Immobilized HRP is a suitable
candidate for wastewater treatment.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "27th International Conference Ecological Truth and Environmental Research",
title = "IMMOBILIZATION OF TYRAMINE-HRP ONTO TYRAMIDECARBOXYMETHYL CELLULOSE MATRIX FOR WASTEWATER TREATMENT",
pages = "224-227",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1657"
}

Prokopijević, M., Pantić, N., Spasojević, D., Prodanović, O., Simonović Radosavljević, J., Đikanović, D.,& Prodanović, R.. (2019). IMMOBILIZATION OF TYRAMINE-HRP ONTO TYRAMIDECARBOXYMETHYL CELLULOSE MATRIX FOR WASTEWATER TREATMENT. in 27th International Conference Ecological Truth and Environmental Research
University of Belgrade, Technical Faculty in Bor., 224-227.
https://hdl.handle.net/21.15107/rcub_rimsi_1657

Prokopijević M, Pantić N, Spasojević D, Prodanović O, Simonović Radosavljević J, Đikanović D, Prodanović R. IMMOBILIZATION OF TYRAMINE-HRP ONTO TYRAMIDECARBOXYMETHYL CELLULOSE MATRIX FOR WASTEWATER TREATMENT. in 27th International Conference Ecological Truth and Environmental Research. 2019;:224-227.
https://hdl.handle.net/21.15107/rcub_rimsi_1657 .

Prokopijević, Miloš, Pantić, Nevena, Spasojević, Dragica, Prodanović, Olivera, Simonović Radosavljević, Jasna, Đikanović, Daniela, Prodanović, Radivoje, "IMMOBILIZATION OF TYRAMINE-HRP ONTO TYRAMIDECARBOXYMETHYL CELLULOSE MATRIX FOR WASTEWATER TREATMENT" in 27th International Conference Ecological Truth and Environmental Research (2019):224-227,
https://hdl.handle.net/21.15107/rcub_rimsi_1657 .