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  - 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  - 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  - 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  - 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  - 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 .

TY  - CONF
AU  - Balaz, Ana Marija
AU  - Popov, Neda
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3043
AB  - Phanerochaete chrysosporium is a white rot fungi and it has been known to secrete
flavocytochrome enzyme cellobiose dehydrogenase (CDH, EC 1.1.99.18) which contains
two domains, a flavine domain and cytochrome domain. Flavine domain contains FAD as
prostetic group and its catalytically active domain, whereas cytochrome domain serves as
electrone acceptor. Cellobiose and lactose, as well as other β – 1,4 – linked disaccharides
and oligosaccharides, have been oxidized by the cellobiose dehydrogenase to their
corresponding lactones. CDH can be used for constructing biosensors and therefore
directed evolution has been used to produce more active and stable variants of the enzyme.
Wild type CDH enzyme was expressed in S.cerevisiae INVSc1 cells and used for creation
of saturation mutagenesis libraries at M65, M685 and M738 and screening for increased
oxidative stability. More stable mutants that were found were recloned into Pichia pastoris
KM71H strain for higher expression yield. They were afterwards, expressed in Pichia,
purified and kineticaly characterized.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
T1  - Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain
EP  - 75
SP  - 74
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3043
ER  - 

@conference{
author = "Balaz, Ana Marija and Popov, Neda and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Phanerochaete chrysosporium is a white rot fungi and it has been known to secrete
flavocytochrome enzyme cellobiose dehydrogenase (CDH, EC 1.1.99.18) which contains
two domains, a flavine domain and cytochrome domain. Flavine domain contains FAD as
prostetic group and its catalytically active domain, whereas cytochrome domain serves as
electrone acceptor. Cellobiose and lactose, as well as other β – 1,4 – linked disaccharides
and oligosaccharides, have been oxidized by the cellobiose dehydrogenase to their
corresponding lactones. CDH can be used for constructing biosensors and therefore
directed evolution has been used to produce more active and stable variants of the enzyme.
Wild type CDH enzyme was expressed in S.cerevisiae INVSc1 cells and used for creation
of saturation mutagenesis libraries at M65, M685 and M738 and screening for increased
oxidative stability. More stable mutants that were found were recloned into Pichia pastoris
KM71H strain for higher expression yield. They were afterwards, expressed in Pichia,
purified and kineticaly characterized.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry",
title = "Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain",
pages = "75-74",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3043"
}

Balaz, A. M., Popov, N., Prodanović, O., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
Faculty of Chemistry, Serbian Biochemical Society., 74-75.
https://hdl.handle.net/21.15107/rcub_rimsi_3043

Balaz AM, Popov N, Prodanović O, Ostafe R, Fischer R, Prodanović R. Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry. 2019;:74-75.
https://hdl.handle.net/21.15107/rcub_rimsi_3043 .

Balaz, Ana Marija, Popov, Neda, Prodanović, Olivera, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain" in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry (2019):74-75,
https://hdl.handle.net/21.15107/rcub_rimsi_3043 .

TY  - CONF
AU  - Stanišić, Marija
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2912
AB  - Pectins belong to a group of a plant polysaccharides that are structural components of plant
cell walls. These polysaccharides have big potential for use in the food industry as a
gelling agents and biomedical application due their biocompatibility, biodegradability, low
price, etc. Chemical modifications of pectin are useful methods for introducing various
functional groups, which give pectin hydrogels novel properties. In this study, pectin was
modified by oxidation with sodium periodate at molar ratios of 5, 10 and 15 mol% and
reductive amination with dopamine and sodium cyanoborohydride afterwards. This
modification of pectin was confirmed by UV-VIS and NMR spectroscopy. Dopaminepectins showed gelling properties in the presence of laccase and oxygen. These pectin
derivatives were tested as carriers for laccase immobilization within microbeads formed in
an emulsion based enzymatic polymerization reaction. Laccase was expressed in functional
form in E. coli, isolated and additionally purified. We determined optimal conditions for
immobilization andobtained microbeads with specific activity of 0.0006 IU/mg and 40%
yield of immobilization. The immobilized laccase could be used for various application,
such as decolorization of textile dyes 
.
PB  - Serbian Biochemical Society
C3  - The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
T1  - Dopamine-modified pectins for laccase induced hydrogel formation and immobilization
EP  - 168
SP  - 168
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2912
ER  - 

@conference{
author = "Stanišić, Marija and Popović, Nikolina and Prodanović, Olivera and Prodanović, Radivoje",
year = "2019",
abstract = "Pectins belong to a group of a plant polysaccharides that are structural components of plant
cell walls. These polysaccharides have big potential for use in the food industry as a
gelling agents and biomedical application due their biocompatibility, biodegradability, low
price, etc. Chemical modifications of pectin are useful methods for introducing various
functional groups, which give pectin hydrogels novel properties. In this study, pectin was
modified by oxidation with sodium periodate at molar ratios of 5, 10 and 15 mol% and
reductive amination with dopamine and sodium cyanoborohydride afterwards. This
modification of pectin was confirmed by UV-VIS and NMR spectroscopy. Dopaminepectins showed gelling properties in the presence of laccase and oxygen. These pectin
derivatives were tested as carriers for laccase immobilization within microbeads formed in
an emulsion based enzymatic polymerization reaction. Laccase was expressed in functional
form in E. coli, isolated and additionally purified. We determined optimal conditions for
immobilization andobtained microbeads with specific activity of 0.0006 IU/mg and 40%
yield of immobilization. The immobilized laccase could be used for various application,
such as decolorization of textile dyes 
.",
publisher = "Serbian Biochemical Society",
journal = "The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry",
title = "Dopamine-modified pectins for laccase induced hydrogel formation and immobilization",
pages = "168-168",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2912"
}

Stanišić, M., Popović, N., Prodanović, O.,& Prodanović, R.. (2019). Dopamine-modified pectins for laccase induced hydrogel formation and immobilization. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
Serbian Biochemical Society., 168-168.
https://hdl.handle.net/21.15107/rcub_rimsi_2912

Stanišić M, Popović N, Prodanović O, Prodanović R. Dopamine-modified pectins for laccase induced hydrogel formation and immobilization. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry. 2019;:168-168.
https://hdl.handle.net/21.15107/rcub_rimsi_2912 .

Stanišić, Marija, Popović, Nikolina, Prodanović, Olivera, Prodanović, Radivoje, "Dopamine-modified pectins for laccase induced hydrogel formation and immobilization" in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry (2019):168-168,
https://hdl.handle.net/21.15107/rcub_rimsi_2912 .

TY  - JOUR
AU  - Spasojević, Milica
AU  - Prodanović, Olivera
AU  - Pantić, Nevena
AU  - Popović, Nikolina
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1757
AB  - Strategies based on the enzyme application are increasingly replacing the conventional chemical procedures because of their efficiency, quicker performance and environmental protection. However, natural enzymes can rarely be used in industry since their beneficial features cannot endure the industrial conditions. Additional drawbacks of natural enzymes are their inhibition by reaction products and difficulty to be removed from the reaction mixture. The most promising technique to substantially improve the enzyme properties, such as activity, pH, thermal and organic-solvent stability, reusability and storage stability, in non-natural environments is by the enzyme immobilization. In this review different techniques used to immobilize enzymes to inert carriers were summarized. Different materials of both the organic and inorganic origin were used as carriers for the enzyme immobilization. A class of new materials where the enzyme performance was enhanced by combining different classical materials and shaping in specific forms was also summarized.
PB  - Faculty of Technology Zvornik
T2  - Journal of Engineering & Processing Management
T1  - The enzyme immobilization: Carriers and immobilization methods
EP  - 105
IS  - 2
SP  - 89
VL  - 11
DO  - 10.7251/jepm1902089s
ER  - 

@article{
author = "Spasojević, Milica and Prodanović, Olivera and Pantić, Nevena and Popović, Nikolina and Balaž, Ana Marija and Prodanović, Radivoje",
year = "2019",
abstract = "Strategies based on the enzyme application are increasingly replacing the conventional chemical procedures because of their efficiency, quicker performance and environmental protection. However, natural enzymes can rarely be used in industry since their beneficial features cannot endure the industrial conditions. Additional drawbacks of natural enzymes are their inhibition by reaction products and difficulty to be removed from the reaction mixture. The most promising technique to substantially improve the enzyme properties, such as activity, pH, thermal and organic-solvent stability, reusability and storage stability, in non-natural environments is by the enzyme immobilization. In this review different techniques used to immobilize enzymes to inert carriers were summarized. Different materials of both the organic and inorganic origin were used as carriers for the enzyme immobilization. A class of new materials where the enzyme performance was enhanced by combining different classical materials and shaping in specific forms was also summarized.",
publisher = "Faculty of Technology Zvornik",
journal = "Journal of Engineering & Processing Management",
title = "The enzyme immobilization: Carriers and immobilization methods",
pages = "105-89",
number = "2",
volume = "11",
doi = "10.7251/jepm1902089s"
}

Spasojević, M., Prodanović, O., Pantić, N., Popović, N., Balaž, A. M.,& Prodanović, R.. (2019). The enzyme immobilization: Carriers and immobilization methods. in Journal of Engineering & Processing Management
Faculty of Technology Zvornik., 11(2), 89-105.
https://doi.org/10.7251/jepm1902089s

Spasojević M, Prodanović O, Pantić N, Popović N, Balaž AM, Prodanović R. The enzyme immobilization: Carriers and immobilization methods. in Journal of Engineering & Processing Management. 2019;11(2):89-105.
doi:10.7251/jepm1902089s .

Spasojević, Milica, Prodanović, Olivera, Pantić, Nevena, Popović, Nikolina, Balaž, Ana Marija, Prodanović, Radivoje, "The enzyme immobilization: Carriers and immobilization methods" in Journal of Engineering & Processing Management, 11, no. 2 (2019):89-105,
https://doi.org/10.7251/jepm1902089s . .

TY  - JOUR
AU  - Blazic, Marija
AU  - Balaž, Ana Marija
AU  - Prodanović, Olivera
AU  - Popović, Nikolina
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1240
AB  - Featured Application Developed fluorescent assay and expression system can be used for obtaining improved cellobiose dehydrogenase whole cell biocatalysts for lactobionic acid production and building of biosensors and biofuel cells. Cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium can be used in lactobionic acid production, biosensor for lactose, biofuel cells, lignocellulose degradation, and wound-healing applications. To make it a better biocatalyst, CDH with higher activity in an immobilized form is desirable. For this purpose, CDH was expressed for the first time on the surface of S. cerevisiae EBY100 cells in an active form as a triple mutant tmCDH (D20N, A64T, V592M) and evolved further for higher activity using resazurin-based fluorescent assay. In order to decrease blank reaction of resazurin with yeast cells and to have linear correlation between enzyme activity on the cell surface and fluorescence signal, the assay was optimized with respect to resazurin concentration (0.1 mM), substrate concentration (10 mM lactose and 0.08 mM cellobiose), and pH (6.0). Using optimized assay an error prone PCR gene library of tmCDH was screened. Two mutants with 5 (H5) and 7 mutations (H9) were found having two times higher activity than the parent tmCDH enzyme that already had improved activity compared to wild type CDH whose activity could not be detected on the surface of yeast cells.
PB  - MDPI, Basel
T2  - Applied Sciences-Basel
T1  - Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay
IS  - 7
VL  - 9
DO  - 10.3390/app9071413
ER  - 

@article{
author = "Blazic, Marija and Balaž, Ana Marija and Prodanović, Olivera and Popović, Nikolina and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Featured Application Developed fluorescent assay and expression system can be used for obtaining improved cellobiose dehydrogenase whole cell biocatalysts for lactobionic acid production and building of biosensors and biofuel cells. Cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium can be used in lactobionic acid production, biosensor for lactose, biofuel cells, lignocellulose degradation, and wound-healing applications. To make it a better biocatalyst, CDH with higher activity in an immobilized form is desirable. For this purpose, CDH was expressed for the first time on the surface of S. cerevisiae EBY100 cells in an active form as a triple mutant tmCDH (D20N, A64T, V592M) and evolved further for higher activity using resazurin-based fluorescent assay. In order to decrease blank reaction of resazurin with yeast cells and to have linear correlation between enzyme activity on the cell surface and fluorescence signal, the assay was optimized with respect to resazurin concentration (0.1 mM), substrate concentration (10 mM lactose and 0.08 mM cellobiose), and pH (6.0). Using optimized assay an error prone PCR gene library of tmCDH was screened. Two mutants with 5 (H5) and 7 mutations (H9) were found having two times higher activity than the parent tmCDH enzyme that already had improved activity compared to wild type CDH whose activity could not be detected on the surface of yeast cells.",
publisher = "MDPI, Basel",
journal = "Applied Sciences-Basel",
title = "Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay",
number = "7",
volume = "9",
doi = "10.3390/app9071413"
}

Blazic, M., Balaž, A. M., Prodanović, O., Popović, N., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. in Applied Sciences-Basel
MDPI, Basel., 9(7).
https://doi.org/10.3390/app9071413

Blazic M, Balaž AM, Prodanović O, Popović N, Ostafe R, Fischer R, Prodanović R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. in Applied Sciences-Basel. 2019;9(7).
doi:10.3390/app9071413 .

Blazic, Marija, Balaž, Ana Marija, Prodanović, Olivera, Popović, Nikolina, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay" in Applied Sciences-Basel, 9, no. 7 (2019),
https://doi.org/10.3390/app9071413 . .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Zelenović, Nevena
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1196
AB  - Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52 +/- 25 mu m and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 degrees C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.
PB  - Polymer Soc Korea, Seoul
T2  - Macromolecular Research
T1  - Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation
EP  - 771
IS  - 8
SP  - 764
VL  - 27
DO  - 10.1007/s13233-019-7111-7
ER  - 

@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Zelenović, Nevena and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2019",
abstract = "Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52 +/- 25 mu m and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 degrees C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.",
publisher = "Polymer Soc Korea, Seoul",
journal = "Macromolecular Research",
title = "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation",
pages = "771-764",
number = "8",
volume = "27",
doi = "10.1007/s13233-019-7111-7"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Zelenović, N., Polović, N., Radotić, K.,& Prodanović, R.. (2019). Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research
Polymer Soc Korea, Seoul., 27(8), 764-771.
https://doi.org/10.1007/s13233-019-7111-7

Spasojević D, Prokopijević M, Prodanović O, Zelenović N, Polović N, Radotić K, Prodanović R. Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research. 2019;27(8):764-771.
doi:10.1007/s13233-019-7111-7 .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Zelenović, Nevena, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation" in Macromolecular Research, 27, no. 8 (2019):764-771,
https://doi.org/10.1007/s13233-019-7111-7 . .