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  - 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  - 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 . .

TY  - CONF
AU  - Kovačević, Ana
AU  - Lukić, Ivana
AU  - Marinković, Emilija
AU  - Miljković, Radmila
AU  - Inic-Kanada, Aleksandra
AU  - Spasojević, Dragica
AU  - Radotić, Ksenija
AU  - Stojanović, Marijana M.
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2870
AB  - The dehydrogenate polymer from coniferyl alcohol (DHP; a lignin model compound) in alginate hydrogel (ALG) has been shown to exert a strong antibacterial activity. To broadens a spectrum of potential DHP/ALG application, we aimed this study to evaluate the immunomodulatory activity of DHP/ALG. DHP and ALG were tested separately and in mixture (1:2 w/w) for their impact on in vitro production of cytokines (IL-6, IL-12, and IL-10) and reactive oxygen (ROS) and nitrogen (RNS) species by resident (RMs) and thioglycolate-elicited (TGMs) peritoneal macrophages of BALB/c mice. RMs and TGMs were stimulated (48h) with ALG and DHP in concentrations previously shown to be non-cytotoxic (up to 50 and 25 μg/ml, respectively). DHP/ALG promotes simultaneous production of inflammatory (IL-6, IL-12) and regulatory cytokines by RMs in a positive dose-dependent manner. Production of inflammatory cytokines was stimulated by ALG, while an increase in IL-10 production positively correlated to the concentration of DHP. ALG also stimulated the production of IL-12 by TGMs, which was mirrored in the outcome of ALG/DHP stimulation. The significant increase in the activity of myeloperoxidase (MPO) due to DHP and/or ALG stimulation was recorded in TGMs, while a slight increase in MPO activity in RMs was recorded only upon stimulation with the higher amount of ALG. ALG in a positive dose-dependent manner stimulated the production of ROS and RNS by both RMS and TGMs. In all cases, except ROS production by RMs, the impact of ALG stimulation was mirrored in the outcome of ALG/DHP stimulation. Our results suggest that DHP/ALG exerts an immunomodulatory activity that could complement already reported antimicrobial activity and warrants further investigation on the use of DHP/ALG in the treatment of infectious diseases.
PB  - Institute for Biological Research "Siniša Stanković"
C3  - Immunology at the confluence of multidisciplinary approaches
T1  - Modulation of functional characteristics of murine peritoneal macrophages by dehydrogenate polymer from coniferyl alcohol and alginate
SP  - 129
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2870
ER  - 

@conference{
author = "Kovačević, Ana and Lukić, Ivana and Marinković, Emilija and Miljković, Radmila and Inic-Kanada, Aleksandra and Spasojević, Dragica and Radotić, Ksenija and Stojanović, Marijana M.",
year = "2019",
abstract = "The dehydrogenate polymer from coniferyl alcohol (DHP; a lignin model compound) in alginate hydrogel (ALG) has been shown to exert a strong antibacterial activity. To broadens a spectrum of potential DHP/ALG application, we aimed this study to evaluate the immunomodulatory activity of DHP/ALG. DHP and ALG were tested separately and in mixture (1:2 w/w) for their impact on in vitro production of cytokines (IL-6, IL-12, and IL-10) and reactive oxygen (ROS) and nitrogen (RNS) species by resident (RMs) and thioglycolate-elicited (TGMs) peritoneal macrophages of BALB/c mice. RMs and TGMs were stimulated (48h) with ALG and DHP in concentrations previously shown to be non-cytotoxic (up to 50 and 25 μg/ml, respectively). DHP/ALG promotes simultaneous production of inflammatory (IL-6, IL-12) and regulatory cytokines by RMs in a positive dose-dependent manner. Production of inflammatory cytokines was stimulated by ALG, while an increase in IL-10 production positively correlated to the concentration of DHP. ALG also stimulated the production of IL-12 by TGMs, which was mirrored in the outcome of ALG/DHP stimulation. The significant increase in the activity of myeloperoxidase (MPO) due to DHP and/or ALG stimulation was recorded in TGMs, while a slight increase in MPO activity in RMs was recorded only upon stimulation with the higher amount of ALG. ALG in a positive dose-dependent manner stimulated the production of ROS and RNS by both RMS and TGMs. In all cases, except ROS production by RMs, the impact of ALG stimulation was mirrored in the outcome of ALG/DHP stimulation. Our results suggest that DHP/ALG exerts an immunomodulatory activity that could complement already reported antimicrobial activity and warrants further investigation on the use of DHP/ALG in the treatment of infectious diseases.",
publisher = "Institute for Biological Research "Siniša Stanković"",
journal = "Immunology at the confluence of multidisciplinary approaches",
title = "Modulation of functional characteristics of murine peritoneal macrophages by dehydrogenate polymer from coniferyl alcohol and alginate",
pages = "129",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2870"
}

Kovačević, A., Lukić, I., Marinković, E., Miljković, R., Inic-Kanada, A., Spasojević, D., Radotić, K.,& Stojanović, M. M.. (2019). Modulation of functional characteristics of murine peritoneal macrophages by dehydrogenate polymer from coniferyl alcohol and alginate. in Immunology at the confluence of multidisciplinary approaches
Institute for Biological Research "Siniša Stanković"., 129.
https://hdl.handle.net/21.15107/rcub_rimsi_2870

Kovačević A, Lukić I, Marinković E, Miljković R, Inic-Kanada A, Spasojević D, Radotić K, Stojanović MM. Modulation of functional characteristics of murine peritoneal macrophages by dehydrogenate polymer from coniferyl alcohol and alginate. in Immunology at the confluence of multidisciplinary approaches. 2019;:129.
https://hdl.handle.net/21.15107/rcub_rimsi_2870 .

Kovačević, Ana, Lukić, Ivana, Marinković, Emilija, Miljković, Radmila, Inic-Kanada, Aleksandra, Spasojević, Dragica, Radotić, Ksenija, Stojanović, Marijana M., "Modulation of functional characteristics of murine peritoneal macrophages by dehydrogenate polymer from coniferyl alcohol and alginate" in Immunology at the confluence of multidisciplinary approaches (2019):129,
https://hdl.handle.net/21.15107/rcub_rimsi_2870 .

TY  - CONF
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Gadjanski, Ivana
AU  - Cvetković, Danijela
AU  - Živanović, Marko
AU  - Pavlović, Vladimir
AU  - Filipović, Nenad D.
AU  - Prodanović, Radivoje
PY  - 2017
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3123
AB  - Carboxymethylcellulose (CMC) is water-soluble cellulose ether which is used in food and cosmetics industry. It also
has big potential for use in pharmaceutical products due to its high biocompatibility, biodegradibility, low immunogenicity and
low price. Crosslinked CMC can absorb large amounts of water and swell to form hydrogels with great physical properties.
The need for new biomaterials and hydrogels is growing daily, due to their use in tissue engineering, drug delivery and cell
and enzyme immobilization studies. In this study we modified CMC, in order to get a crosslinkable polymer that can make
hydrogels by chemical and enzymatic means. After periodate oxidation of CMC we obtained CMC with different degrees of
oxidation: 2.5, 5, 10, 15 and 20 mol%. Further modification using reductive amination in the presence of different phenolic
compounds like tyramine, was done. This modification of CMC was confirmed by UV–VIS and FT-IR spectroscopy, while
concentration of phenol and ionizable groups was determined using absorbance at 275 nm and acid–base titration. All CMCtyramines
were able to form hydrogels after cross-linking with horse radish peroxidase (HRP) and hydrogen peroxide. CMC
derivatives have been successfully electrospun and crosslinked afterwards. Due to the introduction of amino groups and
decrease in molecular weight, they were significantly more soluble in water up to 30 % (w/w) compared to native
polysaccharides and their electrospinability also improved. We aim to make nanofibers using tyramine-polysaccharides that
will be more stable in cell culture media after cross-linking covalently and with calcium/barium ions. Diameter of nanofibers
was determined by scanning electron microscopy (SEM). Cross-linked nanofibers that we obtained will be used for tissue
engineering of blood vessels.
PB  - West University of Timișoara
C3  - The Annual International Conference Romanian Society for Biochemistry & Molecular Biology, 8 - 9. June, Temišvar
T1  - MODIFICATION OF CARBOXYMETHYLCELLULOSE WITH PHENOLS FOR PEROXIDASE INDUCED HYDROGELS FORMATION AND ELECTROSPINNING
IS  - 2
SP  - S4_P10
VL  - 26
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3123
ER  - 

@conference{
author = "Popović, Nikolina and Prodanović, Olivera and Gadjanski, Ivana and Cvetković, Danijela and Živanović, Marko and Pavlović, Vladimir and Filipović, Nenad D. and Prodanović, Radivoje",
year = "2017",
abstract = "Carboxymethylcellulose (CMC) is water-soluble cellulose ether which is used in food and cosmetics industry. It also
has big potential for use in pharmaceutical products due to its high biocompatibility, biodegradibility, low immunogenicity and
low price. Crosslinked CMC can absorb large amounts of water and swell to form hydrogels with great physical properties.
The need for new biomaterials and hydrogels is growing daily, due to their use in tissue engineering, drug delivery and cell
and enzyme immobilization studies. In this study we modified CMC, in order to get a crosslinkable polymer that can make
hydrogels by chemical and enzymatic means. After periodate oxidation of CMC we obtained CMC with different degrees of
oxidation: 2.5, 5, 10, 15 and 20 mol%. Further modification using reductive amination in the presence of different phenolic
compounds like tyramine, was done. This modification of CMC was confirmed by UV–VIS and FT-IR spectroscopy, while
concentration of phenol and ionizable groups was determined using absorbance at 275 nm and acid–base titration. All CMCtyramines
were able to form hydrogels after cross-linking with horse radish peroxidase (HRP) and hydrogen peroxide. CMC
derivatives have been successfully electrospun and crosslinked afterwards. Due to the introduction of amino groups and
decrease in molecular weight, they were significantly more soluble in water up to 30 % (w/w) compared to native
polysaccharides and their electrospinability also improved. We aim to make nanofibers using tyramine-polysaccharides that
will be more stable in cell culture media after cross-linking covalently and with calcium/barium ions. Diameter of nanofibers
was determined by scanning electron microscopy (SEM). Cross-linked nanofibers that we obtained will be used for tissue
engineering of blood vessels.",
publisher = "West University of Timișoara",
journal = "The Annual International Conference Romanian Society for Biochemistry & Molecular Biology, 8 - 9. June, Temišvar",
title = "MODIFICATION OF CARBOXYMETHYLCELLULOSE WITH PHENOLS FOR PEROXIDASE INDUCED HYDROGELS FORMATION AND ELECTROSPINNING",
number = "2",
pages = "S4_P10",
volume = "26",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3123"
}

Popović, N., Prodanović, O., Gadjanski, I., Cvetković, D., Živanović, M., Pavlović, V., Filipović, N. D.,& Prodanović, R.. (2017). MODIFICATION OF CARBOXYMETHYLCELLULOSE WITH PHENOLS FOR PEROXIDASE INDUCED HYDROGELS FORMATION AND ELECTROSPINNING. in The Annual International Conference Romanian Society for Biochemistry & Molecular Biology, 8 - 9. June, Temišvar
West University of Timișoara., 26(2), S4_P10.
https://hdl.handle.net/21.15107/rcub_rimsi_3123

Popović N, Prodanović O, Gadjanski I, Cvetković D, Živanović M, Pavlović V, Filipović ND, Prodanović R. MODIFICATION OF CARBOXYMETHYLCELLULOSE WITH PHENOLS FOR PEROXIDASE INDUCED HYDROGELS FORMATION AND ELECTROSPINNING. in The Annual International Conference Romanian Society for Biochemistry & Molecular Biology, 8 - 9. June, Temišvar. 2017;26(2):S4_P10.
https://hdl.handle.net/21.15107/rcub_rimsi_3123 .

Popović, Nikolina, Prodanović, Olivera, Gadjanski, Ivana, Cvetković, Danijela, Živanović, Marko, Pavlović, Vladimir, Filipović, Nenad D., Prodanović, Radivoje, "MODIFICATION OF CARBOXYMETHYLCELLULOSE WITH PHENOLS FOR PEROXIDASE INDUCED HYDROGELS FORMATION AND ELECTROSPINNING" in The Annual International Conference Romanian Society for Biochemistry & Molecular Biology, 8 - 9. June, Temišvar, 26, no. 2 (2017):S4_P10,
https://hdl.handle.net/21.15107/rcub_rimsi_3123 .

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Kovacević, Gordana
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2017
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1096
AB  - Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 mu mol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K (m) value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization
EP  - 2290
IS  - 6
SP  - 2281
VL  - 101
DO  - 10.1007/s00253-016-8002-x
ER  - 

@article{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Kovacević, Gordana and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2017",
abstract = "Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 mu mol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K (m) value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization",
pages = "2290-2281",
number = "6",
volume = "101",
doi = "10.1007/s00253-016-8002-x"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Kovacević, G., Polović, N., Radotić, K.,& Prodanović, R.. (2017). Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization. in Applied Microbiology and Biotechnology
Springer, New York., 101(6), 2281-2290.
https://doi.org/10.1007/s00253-016-8002-x

Prokopijević M, Prodanović O, Spasojević D, Kovacević G, Polović N, Radotić K, Prodanović R. Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization. in Applied Microbiology and Biotechnology. 2017;101(6):2281-2290.
doi:10.1007/s00253-016-8002-x .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Kovacević, Gordana, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization" in Applied Microbiology and Biotechnology, 101, no. 6 (2017):2281-2290,
https://doi.org/10.1007/s00253-016-8002-x . .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Zmejkoski, Danica
AU  - Glamočlija, Jasmina
AU  - Nikolic, Milos
AU  - Soković, Marina
AU  - Milošević, Verica Lj.
AU  - Jaric, Ivana
AU  - Stojanović, Marijana
AU  - Marinković, Emilija
AU  - Barisani-Asenbauer, Talin
AU  - Prodanović, Radivoje
AU  - Jovanović, Milos
AU  - Radotić, Ksenija
PY  - 2016
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/983
AB  - Nowadays bacterial resistance to known antibiotics is a serious health problem. In order to achieve more efficient treatment, lately there is an effort to find new substances, such as certain biomaterials, that are non-toxic to humans with antibiotic potential. Lignins and lignin-derived compounds have been proposed to be good candidates for use in medicine and health maintenance. In this study, the antibacterial activity of the lignin model polymer dehydrogenate polymer (DHP) in alginate hydrogel (Alg) was studied. The obtained results show that DHP-Alg has strong antimicrobial activity against several bacterial strains and biofilms and does not have a toxic effect on human epithelial cells. These results strongly suggest its application as a wound healing agent or as an adjunct substance for wound treatments.
PB  - Elsevier, Amsterdam
T2  - International Journal of Antimicrobial Agents
T1  - Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment
EP  - 735
IS  - 6
SP  - 732
VL  - 48
DO  - 10.1016/j.ijantimicag.2016.08.014
ER  - 

@article{
author = "Spasojević, Dragica and Zmejkoski, Danica and Glamočlija, Jasmina and Nikolic, Milos and Soković, Marina and Milošević, Verica Lj. and Jaric, Ivana and Stojanović, Marijana and Marinković, Emilija and Barisani-Asenbauer, Talin and Prodanović, Radivoje and Jovanović, Milos and Radotić, Ksenija",
year = "2016",
abstract = "Nowadays bacterial resistance to known antibiotics is a serious health problem. In order to achieve more efficient treatment, lately there is an effort to find new substances, such as certain biomaterials, that are non-toxic to humans with antibiotic potential. Lignins and lignin-derived compounds have been proposed to be good candidates for use in medicine and health maintenance. In this study, the antibacterial activity of the lignin model polymer dehydrogenate polymer (DHP) in alginate hydrogel (Alg) was studied. The obtained results show that DHP-Alg has strong antimicrobial activity against several bacterial strains and biofilms and does not have a toxic effect on human epithelial cells. These results strongly suggest its application as a wound healing agent or as an adjunct substance for wound treatments.",
publisher = "Elsevier, Amsterdam",
journal = "International Journal of Antimicrobial Agents",
title = "Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment",
pages = "735-732",
number = "6",
volume = "48",
doi = "10.1016/j.ijantimicag.2016.08.014"
}

Spasojević, D., Zmejkoski, D., Glamočlija, J., Nikolic, M., Soković, M., Milošević, V. Lj., Jaric, I., Stojanović, M., Marinković, E., Barisani-Asenbauer, T., Prodanović, R., Jovanović, M.,& Radotić, K.. (2016). Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment. in International Journal of Antimicrobial Agents
Elsevier, Amsterdam., 48(6), 732-735.
https://doi.org/10.1016/j.ijantimicag.2016.08.014

Spasojević D, Zmejkoski D, Glamočlija J, Nikolic M, Soković M, Milošević VL, Jaric I, Stojanović M, Marinković E, Barisani-Asenbauer T, Prodanović R, Jovanović M, Radotić K. Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment. in International Journal of Antimicrobial Agents. 2016;48(6):732-735.
doi:10.1016/j.ijantimicag.2016.08.014 .

Spasojević, Dragica, Zmejkoski, Danica, Glamočlija, Jasmina, Nikolic, Milos, Soković, Marina, Milošević, Verica Lj., Jaric, Ivana, Stojanović, Marijana, Marinković, Emilija, Barisani-Asenbauer, Talin, Prodanović, Radivoje, Jovanović, Milos, Radotić, Ksenija, "Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment" in International Journal of Antimicrobial Agents, 48, no. 6 (2016):732-735,
https://doi.org/10.1016/j.ijantimicag.2016.08.014 . .

TY  - CONF
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stanković, Mira
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2015
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1806
AB  - Toxic aromatic pollutants that are found in various industrial wastewaters pose a serious environmental threat. Current methods for phenol removal have certain disadvantages, such as low efficiency, high cost or generation of even more toxic products. On the other hand enzyme-based treatments are highly selective and efficient. Soybean hull peroxidase (SHP) as well as other class III peroxidases catalyzes oxidation reaction in the presence of hydrogen peroxide, resulting in phenol polymerization and formation of less hazardous
phenolic polymers. As a by-product of the food industry, soybean hulls are inexpensive and readily available source of large quantities of crude peroxidase. The aim of our research was to isolate SHP from soybean
hulls and immobilize it onto a glycidyl methacrylate based carriers using glutaraldehyde method and characterize the resulting product. Immobilized SHP showed dependence upon the pore size of the carrier matrix,with the highest obtained specific activity of 22.8 U g-1 of carrier. Immobilized enzyme proved as an effective phenol removal alternative method with improved thermal and organic solvent stabilities compared to the free form. It also showed greater stability and tolerance to pH fluctuations, showing higher specific activities over a wider pH range. Operational stability was tested by repeated pyrogallol oxidation cycles in a batch reactor. After three cycles, immobilized SHP retained over 60% of the initial activity.
PB  - Serbian Plant Physiology Society, Institute for Biological Research „Siniša Stanković“, University of Belgrade, Bulevar despota Stefana 142, 11060 Belgrade, Serbia
C3  - 2st International Conference on Plant Biology • 21th Symposium of the Serbian Plant Physiology Society
T1  - Characterization of soybean hull peroxidase immobilized on glycidyl methacrylate copolymers
EP  - 18
SP  - 17
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1806
ER  - 

@conference{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Stanković, Mira and Stojanović, Željko and Radotić, Ksenija and Prodanović, Radivoje",
year = "2015",
abstract = "Toxic aromatic pollutants that are found in various industrial wastewaters pose a serious environmental threat. Current methods for phenol removal have certain disadvantages, such as low efficiency, high cost or generation of even more toxic products. On the other hand enzyme-based treatments are highly selective and efficient. Soybean hull peroxidase (SHP) as well as other class III peroxidases catalyzes oxidation reaction in the presence of hydrogen peroxide, resulting in phenol polymerization and formation of less hazardous
phenolic polymers. As a by-product of the food industry, soybean hulls are inexpensive and readily available source of large quantities of crude peroxidase. The aim of our research was to isolate SHP from soybean
hulls and immobilize it onto a glycidyl methacrylate based carriers using glutaraldehyde method and characterize the resulting product. Immobilized SHP showed dependence upon the pore size of the carrier matrix,with the highest obtained specific activity of 22.8 U g-1 of carrier. Immobilized enzyme proved as an effective phenol removal alternative method with improved thermal and organic solvent stabilities compared to the free form. It also showed greater stability and tolerance to pH fluctuations, showing higher specific activities over a wider pH range. Operational stability was tested by repeated pyrogallol oxidation cycles in a batch reactor. After three cycles, immobilized SHP retained over 60% of the initial activity.",
publisher = "Serbian Plant Physiology Society, Institute for Biological Research „Siniša Stanković“, University of Belgrade, Bulevar despota Stefana 142, 11060 Belgrade, Serbia",
journal = "2st International Conference on Plant Biology • 21th Symposium of the Serbian Plant Physiology Society",
title = "Characterization of soybean hull peroxidase immobilized on glycidyl methacrylate copolymers",
pages = "18-17",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1806"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Stanković, M., Stojanović, Ž., Radotić, K.,& Prodanović, R.. (2015). Characterization of soybean hull peroxidase immobilized on glycidyl methacrylate copolymers. in 2st International Conference on Plant Biology • 21th Symposium of the Serbian Plant Physiology Society
Serbian Plant Physiology Society, Institute for Biological Research „Siniša Stanković“, University of Belgrade, Bulevar despota Stefana 142, 11060 Belgrade, Serbia., 17-18.
https://hdl.handle.net/21.15107/rcub_rimsi_1806

Prokopijević M, Prodanović O, Spasojević D, Stanković M, Stojanović Ž, Radotić K, Prodanović R. Characterization of soybean hull peroxidase immobilized on glycidyl methacrylate copolymers. in 2st International Conference on Plant Biology • 21th Symposium of the Serbian Plant Physiology Society. 2015;:17-18.
https://hdl.handle.net/21.15107/rcub_rimsi_1806 .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Stanković, Mira, Stojanović, Željko, Radotić, Ksenija, Prodanović, Radivoje, "Characterization of soybean hull peroxidase immobilized on glycidyl methacrylate copolymers" in 2st International Conference on Plant Biology • 21th Symposium of the Serbian Plant Physiology Society (2015):17-18,
https://hdl.handle.net/21.15107/rcub_rimsi_1806 .

TY  - JOUR
AU  - Djokic, Lidija
AU  - Spasic, Jelena
AU  - Jeremic, Sanja
AU  - Vasiljević, Branka
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
AU  - Nikodinovic-Runic, Jasmina
PY  - 2015
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/854
AB  - The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 85 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene
EP  - 2395
IS  - 12
SP  - 2389
VL  - 38
DO  - 10.1007/s00449-015-1474-8
ER  - 

@article{
author = "Djokic, Lidija and Spasic, Jelena and Jeremic, Sanja and Vasiljević, Branka and Prodanović, Olivera and Prodanović, Radivoje and Nikodinovic-Runic, Jasmina",
year = "2015",
abstract = "The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 85 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene",
pages = "2395-2389",
number = "12",
volume = "38",
doi = "10.1007/s00449-015-1474-8"
}

Djokic, L., Spasic, J., Jeremic, S., Vasiljević, B., Prodanović, O., Prodanović, R.,& Nikodinovic-Runic, J.. (2015). Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene. in Bioprocess and Biosystems Engineering
Springer, New York., 38(12), 2389-2395.
https://doi.org/10.1007/s00449-015-1474-8

Djokic L, Spasic J, Jeremic S, Vasiljević B, Prodanović O, Prodanović R, Nikodinovic-Runic J. Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene. in Bioprocess and Biosystems Engineering. 2015;38(12):2389-2395.
doi:10.1007/s00449-015-1474-8 .

Djokic, Lidija, Spasic, Jelena, Jeremic, Sanja, Vasiljević, Branka, Prodanović, Olivera, Prodanović, Radivoje, Nikodinovic-Runic, Jasmina, "Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene" in Bioprocess and Biosystems Engineering, 38, no. 12 (2015):2389-2395,
https://doi.org/10.1007/s00449-015-1474-8 . .

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Radotić, Ksenija
AU  - Marković, Nevena
AU  - Blazic, Marija
AU  - Prodanović, Radivoje
PY  - 2015
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/841
AB  - Phenol and amino groups were introduced into alginate to different degrees via oxidation with 2.5, 5, 10, 15 and 20 mol% of periodate and reductive amination by tyramine. Modification of alginate with tyramine was confirmed by FTIR spectroscopy and UV-VIS spectroscopy, while concentration of phenol and ionizable groups was determined using absorbance at 275 nm and acid-base titration. All tyramine-alginates were able to form hydrogels after cross-linking with horse radish peroxidase (HRP) and hydrogen peroxide. Tyramine-alginates oxidized with up to 10 mol% of periodate were also capable of forming hydrogels with calcium ions. Tyramine-alginates were tested for HRP immobilization within micro-beads obtained by peroxidase catalyzed droplet polymerization using internal delivery of hydrogen peroxide via glucose oxidase and glucose. Highest activity of immobilized peroxidase was obtained with 20% (w/v) tyramine-alginate obtained via 20 mol% periodate oxidation. Immobilized enzyme was not leaking from the micro-beads and was further kinetically characterized for pyrogallol oxidation. Km for pyrogallol was increased after immobilization from 1.93 mM for soluble HRP to 734 mM for immobilized HRP. The optimum pH was also increased from pH 7.0 to 8.0. Temperature and organic solvent stability improved significantly after immobilization, so that half-life at 70 degrees C increased around four times, while half-life in 80% (v/v) dioxane increased 22 times. After repeated use of 6 times in batch reactor for pyrogallol oxidation immobilized HRP retained 45% of original activity.
PB  - Elsevier Science Bv, Amsterdam
T2  - Reactive & Functional Polymers
T1  - Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization
EP  - 83
SP  - 77
VL  - 93
DO  - 10.1016/j.reactfunctpolym.2015.06.004
ER  - 

@article{
author = "Prodanović, Olivera and Spasojević, Dragica and Prokopijević, Miloš and Radotić, Ksenija and Marković, Nevena and Blazic, Marija and Prodanović, Radivoje",
year = "2015",
abstract = "Phenol and amino groups were introduced into alginate to different degrees via oxidation with 2.5, 5, 10, 15 and 20 mol% of periodate and reductive amination by tyramine. Modification of alginate with tyramine was confirmed by FTIR spectroscopy and UV-VIS spectroscopy, while concentration of phenol and ionizable groups was determined using absorbance at 275 nm and acid-base titration. All tyramine-alginates were able to form hydrogels after cross-linking with horse radish peroxidase (HRP) and hydrogen peroxide. Tyramine-alginates oxidized with up to 10 mol% of periodate were also capable of forming hydrogels with calcium ions. Tyramine-alginates were tested for HRP immobilization within micro-beads obtained by peroxidase catalyzed droplet polymerization using internal delivery of hydrogen peroxide via glucose oxidase and glucose. Highest activity of immobilized peroxidase was obtained with 20% (w/v) tyramine-alginate obtained via 20 mol% periodate oxidation. Immobilized enzyme was not leaking from the micro-beads and was further kinetically characterized for pyrogallol oxidation. Km for pyrogallol was increased after immobilization from 1.93 mM for soluble HRP to 734 mM for immobilized HRP. The optimum pH was also increased from pH 7.0 to 8.0. Temperature and organic solvent stability improved significantly after immobilization, so that half-life at 70 degrees C increased around four times, while half-life in 80% (v/v) dioxane increased 22 times. After repeated use of 6 times in batch reactor for pyrogallol oxidation immobilized HRP retained 45% of original activity.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Reactive & Functional Polymers",
title = "Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization",
pages = "83-77",
volume = "93",
doi = "10.1016/j.reactfunctpolym.2015.06.004"
}

Prodanović, O., Spasojević, D., Prokopijević, M., Radotić, K., Marković, N., Blazic, M.,& Prodanović, R.. (2015). Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization. in Reactive & Functional Polymers
Elsevier Science Bv, Amsterdam., 93, 77-83.
https://doi.org/10.1016/j.reactfunctpolym.2015.06.004

Prodanović O, Spasojević D, Prokopijević M, Radotić K, Marković N, Blazic M, Prodanović R. Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization. in Reactive & Functional Polymers. 2015;93:77-83.
doi:10.1016/j.reactfunctpolym.2015.06.004 .

Prodanović, Olivera, Spasojević, Dragica, Prokopijević, Miloš, Radotić, Ksenija, Marković, Nevena, Blazic, Marija, Prodanović, Radivoje, "Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization" in Reactive & Functional Polymers, 93 (2015):77-83,
https://doi.org/10.1016/j.reactfunctpolym.2015.06.004 . .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Pirtea, Marilen Gabriel
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/808
AB  - Imobilizacija peroksidaze iz rena unutar alginatnih kuglica je poboljšana hemijskom modifikacijom enzima i polisaharidnih lanaca. Peroksidaza i alginat su oksidovani perjodatom i naknadno modifikovani etilendiaminom. Najveća specifična aktivnost od 0,43 U/ml gela i 81% vezane aktivnosti je dobijeno korišćenjem aminovane peroksidaze i alginata oksidovanog perjodatom. Imobilizovani enzim je zadržao 75% originalne aktivnosti nakon 2 dana inkubacije u 80% (v/v) dioksanu i imao je povećanu aktivnost pri baznim pH vrednostima u poređenju sa nativnim enzimom. Tokom višestruke upotrebe u šaržnom reaktoru za oksidaciju pirogalola imobilizovana peroksidaza je zadržala 75% početne aktivnosti.
AB  - Immobilization of horseradish peroxidase (HRP) within alginate beads was enabled by chemical modification of the enzyme and polysaccharide chains. HRP and alginate were oxidized by periodate and subsequently modified with ethylenediamine. Highest specific activity of 0.43 U/ml of gel and 81% of bound enzyme activity was obtained using aminated HRP and alginate oxidized by periodate. Immobilized enzyme retained 75% of its original activity after 2 days of incubation in 80% (v/v) dioxane and had increased activity in basic solutions compared to native enzyme. During repeated use in batch reactor for pyrogallol oxidation immobilized peroxidase retained 75% of its original activity.
PB  - Savez hemijskih inženjera, Beograd
T2  - Hemijska Industrija
T1  - Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica
T1  - Immobilization of chemically modified horseradish peroxidase within activated alginate beads
EP  - 122
IS  - 1
SP  - 117
VL  - 68
DO  - 10.2298/HEMIND121122036S
ER  - 

@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Pirtea, Marilen Gabriel and Radotić, Ksenija and Prodanović, Radivoje",
year = "2014",
abstract = "Imobilizacija peroksidaze iz rena unutar alginatnih kuglica je poboljšana hemijskom modifikacijom enzima i polisaharidnih lanaca. Peroksidaza i alginat su oksidovani perjodatom i naknadno modifikovani etilendiaminom. Najveća specifična aktivnost od 0,43 U/ml gela i 81% vezane aktivnosti je dobijeno korišćenjem aminovane peroksidaze i alginata oksidovanog perjodatom. Imobilizovani enzim je zadržao 75% originalne aktivnosti nakon 2 dana inkubacije u 80% (v/v) dioksanu i imao je povećanu aktivnost pri baznim pH vrednostima u poređenju sa nativnim enzimom. Tokom višestruke upotrebe u šaržnom reaktoru za oksidaciju pirogalola imobilizovana peroksidaza je zadržala 75% početne aktivnosti., Immobilization of horseradish peroxidase (HRP) within alginate beads was enabled by chemical modification of the enzyme and polysaccharide chains. HRP and alginate were oxidized by periodate and subsequently modified with ethylenediamine. Highest specific activity of 0.43 U/ml of gel and 81% of bound enzyme activity was obtained using aminated HRP and alginate oxidized by periodate. Immobilized enzyme retained 75% of its original activity after 2 days of incubation in 80% (v/v) dioxane and had increased activity in basic solutions compared to native enzyme. During repeated use in batch reactor for pyrogallol oxidation immobilized peroxidase retained 75% of its original activity.",
publisher = "Savez hemijskih inženjera, Beograd",
journal = "Hemijska Industrija",
title = "Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica, Immobilization of chemically modified horseradish peroxidase within activated alginate beads",
pages = "122-117",
number = "1",
volume = "68",
doi = "10.2298/HEMIND121122036S"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Pirtea, M. G., Radotić, K.,& Prodanović, R.. (2014). Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica. in Hemijska Industrija
Savez hemijskih inženjera, Beograd., 68(1), 117-122.
https://doi.org/10.2298/HEMIND121122036S

Spasojević D, Prokopijević M, Prodanović O, Pirtea MG, Radotić K, Prodanović R. Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica. in Hemijska Industrija. 2014;68(1):117-122.
doi:10.2298/HEMIND121122036S .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Pirtea, Marilen Gabriel, Radotić, Ksenija, Prodanović, Radivoje, "Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica" in Hemijska Industrija, 68, no. 1 (2014):117-122,
https://doi.org/10.2298/HEMIND121122036S . .

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stojanović, Zeljko P
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/754
AB  - Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics
EP  - 804
IS  - 5
SP  - 799
VL  - 37
DO  - 10.1007/s00449-013-1050-z
ER  - 

@article{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Stojanović, Zeljko P and Radotić, Ksenija and Prodanović, Radivoje",
year = "2014",
abstract = "Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics",
pages = "804-799",
number = "5",
volume = "37",
doi = "10.1007/s00449-013-1050-z"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Stojanović, Z. P., Radotić, K.,& Prodanović, R.. (2014). Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. in Bioprocess and Biosystems Engineering
Springer, New York., 37(5), 799-804.
https://doi.org/10.1007/s00449-013-1050-z

Prokopijević M, Prodanović O, Spasojević D, Stojanović ZP, Radotić K, Prodanović R. Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. in Bioprocess and Biosystems Engineering. 2014;37(5):799-804.
doi:10.1007/s00449-013-1050-z .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Stojanović, Zeljko P, Radotić, Ksenija, Prodanović, Radivoje, "Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics" in Bioprocess and Biosystems Engineering, 37, no. 5 (2014):799-804,
https://doi.org/10.1007/s00449-013-1050-z . .

TY  - CONF
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Marinković, Emilija
AU  - Prodanović, Radivoje
PY  - 2013
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1803
AB  - Wastewater treatment is a current and important environmental issue. Phenolic compounds most of which are
toxic and many even carcinogens, found in various polluted waters are non-biodegradable and present a serious
health hazard. Enzymatic treatment, using peroxidase and H2O2, provides a highly selective and efficient alternative
to current phenol removal methods, with low energy requirements and minimal environmental impact.
Soybean hull peroxidase (SHP) isolated from soybean hulls, which are inexpensive agricultural waste products,
offers a cheap source of crude enzyme available for various applications. In this study we used macroporous
glycidyl methacrylate based copolymers with various surface characteristics and mean pore size diameter ranging
from 40-200 nm as carriers and compared two different immobilization methods for SHP – glutaraldehyde
and periodate. Our results demonstrate that SHP immobilization with both methods is influenced by the pore
size of the carrier matrix with both the specific activity of the immobilized enzyme and immobilization yeald
increased with pore size. Glutaraldehyde immobilization method proved to be substantially better than periodate
with the highest specific activities obtained 22.8 U/g and 3.4 U/g of carrier respectively. Thermal stability
at 85°C and stability in 80% dioxane solution indicate a stabilization of the immobilized enzyme compared to
the free form. Although having the same pH optimum, immobilized enzyme operates over a broader pH range.
Obtained biocatalyst shows an increased specific activity, higher thermal and organic solvent stability and operates
over wider pH range and it’s suitable for wastewater treatment.
PB  - MTG - Topgraf Velika Gorica
C3  - 4th Croatian Botanical Symposium with international participation, Split 2013
T1  - Different immobilization methods of soybean hull peroxidase on macroporous glycidyl methacrylate copolymers
SP  - 90
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1803
ER  - 

@conference{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Stojanović, Željko and Radotić, Ksenija and Marinković, Emilija and Prodanović, Radivoje",
year = "2013",
abstract = "Wastewater treatment is a current and important environmental issue. Phenolic compounds most of which are
toxic and many even carcinogens, found in various polluted waters are non-biodegradable and present a serious
health hazard. Enzymatic treatment, using peroxidase and H2O2, provides a highly selective and efficient alternative
to current phenol removal methods, with low energy requirements and minimal environmental impact.
Soybean hull peroxidase (SHP) isolated from soybean hulls, which are inexpensive agricultural waste products,
offers a cheap source of crude enzyme available for various applications. In this study we used macroporous
glycidyl methacrylate based copolymers with various surface characteristics and mean pore size diameter ranging
from 40-200 nm as carriers and compared two different immobilization methods for SHP – glutaraldehyde
and periodate. Our results demonstrate that SHP immobilization with both methods is influenced by the pore
size of the carrier matrix with both the specific activity of the immobilized enzyme and immobilization yeald
increased with pore size. Glutaraldehyde immobilization method proved to be substantially better than periodate
with the highest specific activities obtained 22.8 U/g and 3.4 U/g of carrier respectively. Thermal stability
at 85°C and stability in 80% dioxane solution indicate a stabilization of the immobilized enzyme compared to
the free form. Although having the same pH optimum, immobilized enzyme operates over a broader pH range.
Obtained biocatalyst shows an increased specific activity, higher thermal and organic solvent stability and operates
over wider pH range and it’s suitable for wastewater treatment.",
publisher = "MTG - Topgraf Velika Gorica",
journal = "4th Croatian Botanical Symposium with international participation, Split 2013",
title = "Different immobilization methods of soybean hull peroxidase on macroporous glycidyl methacrylate copolymers",
pages = "90",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1803"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Stojanović, Ž., Radotić, K., Marinković, E.,& Prodanović, R.. (2013). Different immobilization methods of soybean hull peroxidase on macroporous glycidyl methacrylate copolymers. in 4th Croatian Botanical Symposium with international participation, Split 2013
MTG - Topgraf Velika Gorica., 90.
https://hdl.handle.net/21.15107/rcub_rimsi_1803

Prokopijević M, Prodanović O, Spasojević D, Stojanović Ž, Radotić K, Marinković E, Prodanović R. Different immobilization methods of soybean hull peroxidase on macroporous glycidyl methacrylate copolymers. in 4th Croatian Botanical Symposium with international participation, Split 2013. 2013;:90.
https://hdl.handle.net/21.15107/rcub_rimsi_1803 .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Stojanović, Željko, Radotić, Ksenija, Marinković, Emilija, Prodanović, Radivoje, "Different immobilization methods of soybean hull peroxidase on macroporous glycidyl methacrylate copolymers" in 4th Croatian Botanical Symposium with international participation, Split 2013 (2013):90,
https://hdl.handle.net/21.15107/rcub_rimsi_1803 .

TY  - JOUR
AU  - Blazic, Marija B
AU  - Kovacević, Gordana
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Gavrovic-Jankulović, Marija D
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2013
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/705
AB  - Glucose oxidase (GOx) catalyzes the oxidation of glucose to form gluconic acid and hydrogen peroxide, a reaction with important applications in food preservation, the manufacture of cosmetics and pharmaceuticals, and the development of glucose monitoring devices and biofuel cells. We expressed Aspergillus niger wild type GOx and the B11 mutant, which has twice the activity of the wild type enzyme at pH 5.5, as C-terminal fusions with the Saccharomyces cerevisiae Aga2 protein, allowing the fusion proteins to be displayed on the surface of yeast EBY100 cells. After expression, we extracted the proteins from the yeast cell wall and purified them by ion-exchange chromatography and ultrafiltration. This produced a broad 100-140 kDa band by denaturing SDS-PAGE and a high-molecular-weight band by native PAGE corresponding to the activity band revealed by zymography. The wild type and B11 fusion proteins had k(cat) values of 33.3 and 61.3 s(-1) and K-m values for glucose of 33.4 and 27.9 mM, respectively. The pH optimum for both enzymes was 5.0. The kinetic properties of the fusion proteins displayed the same ratio as their native counterparts, confirming that yeast surface display is suitable for the high-throughput directed evolution of GOx using flow cytometry for selection. Aga2-GOx fusion proteins in the yeast cell wall could also be used as immobilized catalysts for the production of gluconic acid.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Protein Expression and Purification
T1  - Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases
EP  - 180
IS  - 2
SP  - 175
VL  - 89
DO  - 10.1016/j.pep.2013.03.014
ER  - 

@article{
author = "Blazic, Marija B and Kovacević, Gordana and Prodanović, Olivera and Ostafe, Raluca and Gavrovic-Jankulović, Marija D and Fischer, Rainer and Prodanović, Radivoje",
year = "2013",
abstract = "Glucose oxidase (GOx) catalyzes the oxidation of glucose to form gluconic acid and hydrogen peroxide, a reaction with important applications in food preservation, the manufacture of cosmetics and pharmaceuticals, and the development of glucose monitoring devices and biofuel cells. We expressed Aspergillus niger wild type GOx and the B11 mutant, which has twice the activity of the wild type enzyme at pH 5.5, as C-terminal fusions with the Saccharomyces cerevisiae Aga2 protein, allowing the fusion proteins to be displayed on the surface of yeast EBY100 cells. After expression, we extracted the proteins from the yeast cell wall and purified them by ion-exchange chromatography and ultrafiltration. This produced a broad 100-140 kDa band by denaturing SDS-PAGE and a high-molecular-weight band by native PAGE corresponding to the activity band revealed by zymography. The wild type and B11 fusion proteins had k(cat) values of 33.3 and 61.3 s(-1) and K-m values for glucose of 33.4 and 27.9 mM, respectively. The pH optimum for both enzymes was 5.0. The kinetic properties of the fusion proteins displayed the same ratio as their native counterparts, confirming that yeast surface display is suitable for the high-throughput directed evolution of GOx using flow cytometry for selection. Aga2-GOx fusion proteins in the yeast cell wall could also be used as immobilized catalysts for the production of gluconic acid.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Protein Expression and Purification",
title = "Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases",
pages = "180-175",
number = "2",
volume = "89",
doi = "10.1016/j.pep.2013.03.014"
}

Blazic, M. B., Kovacević, G., Prodanović, O., Ostafe, R., Gavrovic-Jankulović, M. D., Fischer, R.,& Prodanović, R.. (2013). Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases. in Protein Expression and Purification
Academic Press Inc Elsevier Science, San Diego., 89(2), 175-180.
https://doi.org/10.1016/j.pep.2013.03.014

Blazic MB, Kovacević G, Prodanović O, Ostafe R, Gavrovic-Jankulović MD, Fischer R, Prodanović R. Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases. in Protein Expression and Purification. 2013;89(2):175-180.
doi:10.1016/j.pep.2013.03.014 .

Blazic, Marija B, Kovacević, Gordana, Prodanović, Olivera, Ostafe, Raluca, Gavrovic-Jankulović, Marija D, Fischer, Rainer, Prodanović, Radivoje, "Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases" in Protein Expression and Purification, 89, no. 2 (2013):175-180,
https://doi.org/10.1016/j.pep.2013.03.014 . .

TY  - CONF
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2012
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3122
AB  - Phenols are considered priority pollutants of wastewaters, they are non-biodegradable and the problem of their
removal is a current and important enviromental issue. Enzymatic treatment of wastewaters using peroxidase
and H2O2 is highly effective and selective method. Soybean hulls offer cheap source of large amounts of crude
enzyme (soybean hull peroxidase - SHP), which can be used for this purpose. The aim of this research was to
test different macroporous carriers for immobilization of soybean hull peroxidase. Our data demonstrate that
SHP immobilization using glutaraldehyde activation is influenced by the pore size of the macroporous glycidyl
methacrylate matrix. Both specific activity of the immobilized enzyme and immobilization yeald were increased
with the increase in pore size, and the highest specific activity obtained was 22,8 U/g of carrier.
C3  - 50. Savetovanje Srpskog hemijskog društva, Beograd, 14. i 15.juni 2012
T1  - Poređenje imobilizacije peroksidaze soje na različite glicidil metakrilat polimere
EP  - 194
SP  - 191
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3122
ER  - 

@conference{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Stojanović, Željko and Radotić, Ksenija and Prodanović, Radivoje",
year = "2012",
abstract = "Phenols are considered priority pollutants of wastewaters, they are non-biodegradable and the problem of their
removal is a current and important enviromental issue. Enzymatic treatment of wastewaters using peroxidase
and H2O2 is highly effective and selective method. Soybean hulls offer cheap source of large amounts of crude
enzyme (soybean hull peroxidase - SHP), which can be used for this purpose. The aim of this research was to
test different macroporous carriers for immobilization of soybean hull peroxidase. Our data demonstrate that
SHP immobilization using glutaraldehyde activation is influenced by the pore size of the macroporous glycidyl
methacrylate matrix. Both specific activity of the immobilized enzyme and immobilization yeald were increased
with the increase in pore size, and the highest specific activity obtained was 22,8 U/g of carrier.",
journal = "50. Savetovanje Srpskog hemijskog društva, Beograd, 14. i 15.juni 2012",
title = "Poređenje imobilizacije peroksidaze soje na različite glicidil metakrilat polimere",
pages = "194-191",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3122"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Stojanović, Ž., Radotić, K.,& Prodanović, R.. (2012). Poređenje imobilizacije peroksidaze soje na različite glicidil metakrilat polimere. in 50. Savetovanje Srpskog hemijskog društva, Beograd, 14. i 15.juni 2012, 191-194.
https://hdl.handle.net/21.15107/rcub_rimsi_3122

Prokopijević M, Prodanović O, Spasojević D, Stojanović Ž, Radotić K, Prodanović R. Poređenje imobilizacije peroksidaze soje na različite glicidil metakrilat polimere. in 50. Savetovanje Srpskog hemijskog društva, Beograd, 14. i 15.juni 2012. 2012;:191-194.
https://hdl.handle.net/21.15107/rcub_rimsi_3122 .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Stojanović, Željko, Radotić, Ksenija, Prodanović, Radivoje, "Poređenje imobilizacije peroksidaze soje na različite glicidil metakrilat polimere" in 50. Savetovanje Srpskog hemijskog društva, Beograd, 14. i 15.juni 2012 (2012):191-194,
https://hdl.handle.net/21.15107/rcub_rimsi_3122 .

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Stojanović, Zeljko P
AU  - Radotić, Ksenija
AU  - Knezevic-Jugović, Zorica D
AU  - Prodanović, Radivoje
PY  - 2012
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/586
AB  - A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.
PB  - Springer, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers
EP  - 1301
IS  - 5
SP  - 1288
VL  - 168
DO  - 10.1007/s12010-012-9857-7
ER  - 

@article{
author = "Prodanović, Olivera and Prokopijević, Miloš and Spasojević, Dragica and Stojanović, Zeljko P and Radotić, Ksenija and Knezevic-Jugović, Zorica D and Prodanović, Radivoje",
year = "2012",
abstract = "A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.",
publisher = "Springer, New York",
journal = "Applied Biochemistry and Biotechnology",
title = "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers",
pages = "1301-1288",
number = "5",
volume = "168",
doi = "10.1007/s12010-012-9857-7"
}

Prodanović, O., Prokopijević, M., Spasojević, D., Stojanović, Z. P., Radotić, K., Knezevic-Jugović, Z. D.,& Prodanović, R.. (2012). Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology
Springer, New York., 168(5), 1288-1301.
https://doi.org/10.1007/s12010-012-9857-7

Prodanović O, Prokopijević M, Spasojević D, Stojanović ZP, Radotić K, Knezevic-Jugović ZD, Prodanović R. Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology. 2012;168(5):1288-1301.
doi:10.1007/s12010-012-9857-7 .

Prodanović, Olivera, Prokopijević, Miloš, Spasojević, Dragica, Stojanović, Zeljko P, Radotić, Ksenija, Knezevic-Jugović, Zorica D, Prodanović, Radivoje, "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers" in Applied Biochemistry and Biotechnology, 168, no. 5 (2012):1288-1301,
https://doi.org/10.1007/s12010-012-9857-7 . .

TY  - JOUR
AU  - Milosavić, Nenad B
AU  - Bogdanović Pristov, Jelena
AU  - Velicković, Dusan V
AU  - Dimitrijević, Aleksandra S
AU  - Kalauzi, Aleksandar
AU  - Radotić, Ksenija
PY  - 2012
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/574
AB  - BACKGROUND: A totally new approach has been applied for mathematical modeling of the enzyme activity/pH relationship, for quantification and distribution of enzyme activity in and out of carrier pores. This is a very simple and elegant method for determination of the distribution of enzyme molecules on the surface and inside the particles, simply through measurement of enzyme activity at different pH values. RESULTS: Amyloglucosidase (AG) from Aspergillus niger was covalently immobilized onto poly(GMA-co-EGDMA) by the glutaraldehyde and periodate methods. Mathematical modeling of the pH optima for two types of covalently immobilized AG resulted in higher enzyme amounts on the surface within periodate immobilizate (67%) in comparison with glutaraldehyde immobilizate (53%). These values are modified to 64.25% for periodate immobilizate and 49.95% for glutaraldehyde immobilizate when diffusion effects are taken into account. CONCLUSION: The mathematical model applied enabled observation of the difference between the two types of coupling agents and different immobilization procedures throughout quantification of the immobilized enzyme on the matrix surface and inside pores.
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of Chemical Technology and Biotechnology
T1  - Study of the covalently immobilized amyloglucosidase on macroporous polymer by mathematical modeling of the pH optima
EP  - 1457
IS  - 10
SP  - 1450
VL  - 87
DO  - 10.1002/jctb.3768
ER  - 

@article{
author = "Milosavić, Nenad B and Bogdanović Pristov, Jelena and Velicković, Dusan V and Dimitrijević, Aleksandra S and Kalauzi, Aleksandar and Radotić, Ksenija",
year = "2012",
abstract = "BACKGROUND: A totally new approach has been applied for mathematical modeling of the enzyme activity/pH relationship, for quantification and distribution of enzyme activity in and out of carrier pores. This is a very simple and elegant method for determination of the distribution of enzyme molecules on the surface and inside the particles, simply through measurement of enzyme activity at different pH values. RESULTS: Amyloglucosidase (AG) from Aspergillus niger was covalently immobilized onto poly(GMA-co-EGDMA) by the glutaraldehyde and periodate methods. Mathematical modeling of the pH optima for two types of covalently immobilized AG resulted in higher enzyme amounts on the surface within periodate immobilizate (67%) in comparison with glutaraldehyde immobilizate (53%). These values are modified to 64.25% for periodate immobilizate and 49.95% for glutaraldehyde immobilizate when diffusion effects are taken into account. CONCLUSION: The mathematical model applied enabled observation of the difference between the two types of coupling agents and different immobilization procedures throughout quantification of the immobilized enzyme on the matrix surface and inside pores.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of Chemical Technology and Biotechnology",
title = "Study of the covalently immobilized amyloglucosidase on macroporous polymer by mathematical modeling of the pH optima",
pages = "1457-1450",
number = "10",
volume = "87",
doi = "10.1002/jctb.3768"
}

Milosavić, N. B., Bogdanović Pristov, J., Velicković, D. V., Dimitrijević, A. S., Kalauzi, A.,& Radotić, K.. (2012). Study of the covalently immobilized amyloglucosidase on macroporous polymer by mathematical modeling of the pH optima. in Journal of Chemical Technology and Biotechnology
Wiley-Blackwell, Hoboken., 87(10), 1450-1457.
https://doi.org/10.1002/jctb.3768

Milosavić NB, Bogdanović Pristov J, Velicković DV, Dimitrijević AS, Kalauzi A, Radotić K. Study of the covalently immobilized amyloglucosidase on macroporous polymer by mathematical modeling of the pH optima. in Journal of Chemical Technology and Biotechnology. 2012;87(10):1450-1457.
doi:10.1002/jctb.3768 .

Milosavić, Nenad B, Bogdanović Pristov, Jelena, Velicković, Dusan V, Dimitrijević, Aleksandra S, Kalauzi, Aleksandar, Radotić, Ksenija, "Study of the covalently immobilized amyloglucosidase on macroporous polymer by mathematical modeling of the pH optima" in Journal of Chemical Technology and Biotechnology, 87, no. 10 (2012):1450-1457,
https://doi.org/10.1002/jctb.3768 . .