TY  - CONF
AU  - Stanišić, Marija D.
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Senćanski, Milan
AU  - Mitić, Dragana
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5751
AB  - Novel industrial biocatalysts are needed which can offer advantages over traditional chemical processes with respect to sustainability, process efficiency, and reduced negative impact on the environment. Implementation of either native or mutated enzymes for various industrial applications is currently limited due to a lack of protein stability in harsh conditions. Metal-organic frameworks (MOFs), known for their ultra-high porosity and crystallinity, are perfect host materials that can protect guest enzymes from inhospitable external environments. Herein we show that the surface charge and chemistry of a protein determine its ability to seed MOF growth. We demonstrate that chemical modification of carbohydrate parts on the protein surface is an effective method for controlling biomimetic mineralization by zeolitic imidazolate framework-8 (ZIF-8). Protein charge, mixing of reactants, and stirring speed have been demonstrated to play important roles in controlling biomineralization reaction rate, particle shape, and morphology. This study highlights the important role played by protein surface chemistry in encapsulation and outlines a general method for facilitating the biomimetic mineralization of glycoproteins.
C3  - EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland
T1  - Efficient enzyme@MOF composites for biocatalysis
SP  - 138
EP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5751
ER  - 

@conference{
author = "Stanišić, Marija D. and Ristić, Predrag and Balaž, Ana Marija and Senćanski, Milan and Mitić, Dragana and Prodanović, Radivoje and Todorović, Tamara",
year = "2022",
abstract = "Novel industrial biocatalysts are needed which can offer advantages over traditional chemical processes with respect to sustainability, process efficiency, and reduced negative impact on the environment. Implementation of either native or mutated enzymes for various industrial applications is currently limited due to a lack of protein stability in harsh conditions. Metal-organic frameworks (MOFs), known for their ultra-high porosity and crystallinity, are perfect host materials that can protect guest enzymes from inhospitable external environments. Herein we show that the surface charge and chemistry of a protein determine its ability to seed MOF growth. We demonstrate that chemical modification of carbohydrate parts on the protein surface is an effective method for controlling biomimetic mineralization by zeolitic imidazolate framework-8 (ZIF-8). Protein charge, mixing of reactants, and stirring speed have been demonstrated to play important roles in controlling biomineralization reaction rate, particle shape, and morphology. This study highlights the important role played by protein surface chemistry in encapsulation and outlines a general method for facilitating the biomimetic mineralization of glycoproteins.",
journal = "EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland",
title = "Efficient enzyme@MOF composites for biocatalysis",
pages = "138-138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5751"
}

Stanišić, M. D., Ristić, P., Balaž, A. M., Senćanski, M., Mitić, D., Prodanović, R.,& Todorović, T.. (2022). Efficient enzyme@MOF composites for biocatalysis. in EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland, 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5751

Stanišić MD, Ristić P, Balaž AM, Senćanski M, Mitić D, Prodanović R, Todorović T. Efficient enzyme@MOF composites for biocatalysis. in EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5751 .

Stanišić, Marija D., Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Mitić, Dragana, Prodanović, Radivoje, Todorović, Tamara, "Efficient enzyme@MOF composites for biocatalysis" in EUROBIOTECH 8th Central European Congress of Life Sciences, 20-22 June 2022, Krakow, Poland (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5751 .

TY  - CONF
AU  - Ristić, Predrag
AU  - Stanišić, Marija D.
AU  - Đokić, Veljko
AU  - Balaž, Ana Marija
AU  - Mitić, Dragana
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5753
AB  - The durability of enzymes in harsh conditions can be enhanced by immobilization within metal-organic frameworks
(MOFs) via a process called biomimetic mineralisation. Zeolitic imidazolate framework-8 (ZIF-8) is widely used as a
protective coating to encapsulate proteins. The formation of nucleation centres and further biocomposite particle
growth is entirely governed by the pure electrostatic interactions between the protein’s surface and positively charged
Zn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modification
of surface amino acid residues can lead to a rapid biocomposite formation. However, a chemical modification of
carbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the present
study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidation
of GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule. Biomineralization
experiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability of
the ZIF-8 biocomposites.
C3  - 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece
T1  - Periodate oxidized glucose oxidase@ZIF-8 nanocomposite
SP  - 138
EP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5753
ER  - 

@conference{
author = "Ristić, Predrag and Stanišić, Marija D. and Đokić, Veljko and Balaž, Ana Marija and Mitić, Dragana and Prodanović, Radivoje and Todorović, Tamara",
year = "2022",
abstract = "The durability of enzymes in harsh conditions can be enhanced by immobilization within metal-organic frameworks
(MOFs) via a process called biomimetic mineralisation. Zeolitic imidazolate framework-8 (ZIF-8) is widely used as a
protective coating to encapsulate proteins. The formation of nucleation centres and further biocomposite particle
growth is entirely governed by the pure electrostatic interactions between the protein’s surface and positively charged
Zn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modification
of surface amino acid residues can lead to a rapid biocomposite formation. However, a chemical modification of
carbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the present
study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidation
of GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule. Biomineralization
experiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability of
the ZIF-8 biocomposites.",
journal = "19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece",
title = "Periodate oxidized glucose oxidase@ZIF-8 nanocomposite",
pages = "138-138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5753"
}

Ristić, P., Stanišić, M. D., Đokić, V., Balaž, A. M., Mitić, D., Prodanović, R.,& Todorović, T.. (2022). Periodate oxidized glucose oxidase@ZIF-8 nanocomposite. in 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece, 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5753

Ristić P, Stanišić MD, Đokić V, Balaž AM, Mitić D, Prodanović R, Todorović T. Periodate oxidized glucose oxidase@ZIF-8 nanocomposite. in 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5753 .

Ristić, Predrag, Stanišić, Marija D., Đokić, Veljko, Balaž, Ana Marija, Mitić, Dragana, Prodanović, Radivoje, Todorović, Tamara, "Periodate oxidized glucose oxidase@ZIF-8 nanocomposite" in 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5753 .

TY  - THES
AU  - Stanojević, Nataša
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5459
AB  - Enzimi su biokatalizatori koji mogu specifično i efikasno katalizovati veliki broj različitih hemijskih reakcija. Zbog svojih osobina nalaze širok spektar primjene u svim granama industrije. Međutim, uslovi pod kojim je potreban rad enzima, najčešće nisu povoljni za strukturu i funkciju biokatalizatora. Proteinski inženjering omogućava dizajn proteina sa modifikacijama koje poboljšavaju osobine enzima i prilagođavaju ih ciljanoj upotrebi.
Cilj ovog rada bio je dobijanje aktivnijeg oblika peroksidaze iz rena (C1A) uz pomoć proteinskog inženjeringa. Mjesto specifičnom mutacijom moguće je uticati direktno na specifične osobine enzima u cilju njihovih poboljšanja. Peroksidaza iz rena je dobro proučen protein, sa nizom primjena u analitičkim metodama, bioremedijaciji, organskim sintezama i sl. Stoga proizvodnja aktivnijeg oblika ovog enzima ima značaj za različite oblasti primjene.
T1  - Heterologna ekspresija i prečišćavanje mutanta R302I peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H
SP  - 1
EP  - 45
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5459
ER  - 

@mastersthesis{
author = "Stanojević, Nataša",
year = "2022",
abstract = "Enzimi su biokatalizatori koji mogu specifično i efikasno katalizovati veliki broj različitih hemijskih reakcija. Zbog svojih osobina nalaze širok spektar primjene u svim granama industrije. Međutim, uslovi pod kojim je potreban rad enzima, najčešće nisu povoljni za strukturu i funkciju biokatalizatora. Proteinski inženjering omogućava dizajn proteina sa modifikacijama koje poboljšavaju osobine enzima i prilagođavaju ih ciljanoj upotrebi.
Cilj ovog rada bio je dobijanje aktivnijeg oblika peroksidaze iz rena (C1A) uz pomoć proteinskog inženjeringa. Mjesto specifičnom mutacijom moguće je uticati direktno na specifične osobine enzima u cilju njihovih poboljšanja. Peroksidaza iz rena je dobro proučen protein, sa nizom primjena u analitičkim metodama, bioremedijaciji, organskim sintezama i sl. Stoga proizvodnja aktivnijeg oblika ovog enzima ima značaj za različite oblasti primjene.",
title = "Heterologna ekspresija i prečišćavanje mutanta R302I peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H",
pages = "1-45",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5459"
}

Stanojević, N.. (2022). Heterologna ekspresija i prečišćavanje mutanta R302I peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H. , 1-45.
https://hdl.handle.net/21.15107/rcub_cherry_5459

Stanojević N. Heterologna ekspresija i prečišćavanje mutanta R302I peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H. 2022;:1-45.
https://hdl.handle.net/21.15107/rcub_cherry_5459 .

Stanojević, Nataša, "Heterologna ekspresija i prečišćavanje mutanta R302I peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H" (2022):1-45,
https://hdl.handle.net/21.15107/rcub_cherry_5459 .

TY  - THES
AU  - Vlajkov, Nikola M.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5460
AB  - U ovom radu je pPICZA vektor sa ukloniranim mutiranim genom za peroksidazu iz rena, kom
je uvedena mesto specifična mutacija iz aminokiseline izoleucin na poziciji 297 u aminokiseinu
treonin, korišten za transformaciju ćelija Pichia pastoris KM71H, koje su zatim podvrgnute
fermentaciji kako bi se u ekstracelularnom medijumu (fermentacionoj tečnosti) eksprimirao
mutirani enzim peroksidaze iz rena. Eksprimirani enzim peroksidaze iz rena je iz fermentacione
tečnosti prečišćen na DEAE matriksu, pomoću HPLC instrumenta. Da li je uvedena mutacija
dovela do poboljšanja u enzimskoj aktivnosti peroksidaze iz rena testirano je ABTS supstrat
esejem, a dobijeni rezultati su poređeni sa enzimskom aktivnosti „divljeg soja“ enzima
peroksidaze iz rena.
T1  - Heterologna ekspresija i prečišćavanje mutanta I297T peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H
SP  - 1
EP  - 50
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5460
ER  - 

@mastersthesis{
author = "Vlajkov, Nikola M.",
year = "2022",
abstract = "U ovom radu je pPICZA vektor sa ukloniranim mutiranim genom za peroksidazu iz rena, kom
je uvedena mesto specifična mutacija iz aminokiseline izoleucin na poziciji 297 u aminokiseinu
treonin, korišten za transformaciju ćelija Pichia pastoris KM71H, koje su zatim podvrgnute
fermentaciji kako bi se u ekstracelularnom medijumu (fermentacionoj tečnosti) eksprimirao
mutirani enzim peroksidaze iz rena. Eksprimirani enzim peroksidaze iz rena je iz fermentacione
tečnosti prečišćen na DEAE matriksu, pomoću HPLC instrumenta. Da li je uvedena mutacija
dovela do poboljšanja u enzimskoj aktivnosti peroksidaze iz rena testirano je ABTS supstrat
esejem, a dobijeni rezultati su poređeni sa enzimskom aktivnosti „divljeg soja“ enzima
peroksidaze iz rena.",
title = "Heterologna ekspresija i prečišćavanje mutanta I297T peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H",
pages = "1-50",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5460"
}

Vlajkov, N. M.. (2022). Heterologna ekspresija i prečišćavanje mutanta I297T peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H. , 1-50.
https://hdl.handle.net/21.15107/rcub_cherry_5460

Vlajkov NM. Heterologna ekspresija i prečišćavanje mutanta I297T peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H. 2022;:1-50.
https://hdl.handle.net/21.15107/rcub_cherry_5460 .

Vlajkov, Nikola M., "Heterologna ekspresija i prečišćavanje mutanta I297T peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H" (2022):1-50,
https://hdl.handle.net/21.15107/rcub_cherry_5460 .

TY  - THES
AU  - Đajić, Milan
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5461
AB  - Cilj ovog rada je kreiranje mutanta HRP R27L, korišćenjem mjesto specifične mutageneze u cilju povećanja enzimske aktivnosti mutirane varijante enzima u odnosu na wild type formu. Konstruisani mutant je eksprimiran u kvascu Pichia pastoris, a potom je prečišćen i upoređen sa wild type enzimom.
T1  - Heterologna ekspresija i prečišćavanje mutanta R27L peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H
SP  - 1
EP  - 46
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5461
ER  - 

@mastersthesis{
author = "Đajić, Milan",
year = "2022",
abstract = "Cilj ovog rada je kreiranje mutanta HRP R27L, korišćenjem mjesto specifične mutageneze u cilju povećanja enzimske aktivnosti mutirane varijante enzima u odnosu na wild type formu. Konstruisani mutant je eksprimiran u kvascu Pichia pastoris, a potom je prečišćen i upoređen sa wild type enzimom.",
title = "Heterologna ekspresija i prečišćavanje mutanta R27L peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H",
pages = "1-46",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5461"
}

Đajić, M.. (2022). Heterologna ekspresija i prečišćavanje mutanta R27L peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H. , 1-46.
https://hdl.handle.net/21.15107/rcub_cherry_5461

Đajić M. Heterologna ekspresija i prečišćavanje mutanta R27L peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H. 2022;:1-46.
https://hdl.handle.net/21.15107/rcub_cherry_5461 .

Đajić, Milan, "Heterologna ekspresija i prečišćavanje mutanta R27L peroksidaze iz rena izoforme C1A u kvascu Pichia pastoris KM71H" (2022):1-46,
https://hdl.handle.net/21.15107/rcub_cherry_5461 .

TY  - JOUR
AU  - Stanišić, Marija D.
AU  - Popović Kokar, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Ognjanović, Miloš
AU  - Đokić, Veljko R.
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5678
AB  - Many articles in the literature deal with horseradish peroxidase (HRP) biomineralization, but none pay attention to the isoenzyme composition of commercial HRP or the influence of the carbohydrate component of the protein molecule on the biomineralization process. To study the impact of these factors, we performed periodate oxidation of commercial HRP and a purified HRP-C isoform for biomineralization within ZIF-8. With purified HRP, enzyme@ZIF-8 biocomposites with higher activity were obtained, while periodate oxidation of the carbohydrate component of both commercial HRP and purified HRP-C yields biocomposites with very high activity in acetate buffer that does not degrade the ZIF-8 structure. Using acetate instead of phosphate buffer can prevent the false high activity of HRP@ZIF-8 biocomposites caused by the degradation of ZIF-8 coating. At the same time, purification and especially oxidation of the carbohydrate component of enzymes prior to biomineralization lead to significantly improved activity of the biocomposites.
PB  - MDPI
T2  - Polymers
T1  - The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance
VL  - 14
IS  - 22
SP  - 4834
DO  - 10.3390/polym14224834
ER  - 

@article{
author = "Stanišić, Marija D. and Popović Kokar, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Ognjanović, Miloš and Đokić, Veljko R. and Prodanović, Radivoje and Todorović, Tamara",
year = "2022",
abstract = "Many articles in the literature deal with horseradish peroxidase (HRP) biomineralization, but none pay attention to the isoenzyme composition of commercial HRP or the influence of the carbohydrate component of the protein molecule on the biomineralization process. To study the impact of these factors, we performed periodate oxidation of commercial HRP and a purified HRP-C isoform for biomineralization within ZIF-8. With purified HRP, enzyme@ZIF-8 biocomposites with higher activity were obtained, while periodate oxidation of the carbohydrate component of both commercial HRP and purified HRP-C yields biocomposites with very high activity in acetate buffer that does not degrade the ZIF-8 structure. Using acetate instead of phosphate buffer can prevent the false high activity of HRP@ZIF-8 biocomposites caused by the degradation of ZIF-8 coating. At the same time, purification and especially oxidation of the carbohydrate component of enzymes prior to biomineralization lead to significantly improved activity of the biocomposites.",
publisher = "MDPI",
journal = "Polymers",
title = "The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance",
volume = "14",
number = "22",
pages = "4834",
doi = "10.3390/polym14224834"
}

Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2022). The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers
MDPI., 14(22), 4834.
https://doi.org/10.3390/polym14224834

Stanišić MD, Popović Kokar N, Ristić P, Balaž AM, Ognjanović M, Đokić VR, Prodanović R, Todorović T. The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers. 2022;14(22):4834.
doi:10.3390/polym14224834 .

Stanišić, Marija D., Popović Kokar, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Ognjanović, Miloš, Đokić, Veljko R., Prodanović, Radivoje, Todorović, Tamara, "The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance" in Polymers, 14, no. 22 (2022):4834,
https://doi.org/10.3390/polym14224834 . .

TY  - DATA
AU  - Stanišić, Marija D.
AU  - Popović Kokar, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Ognjanović, Miloš
AU  - Đokić, Veljko R.
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5740
T1  - Primary research data for the article: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T. R.. (2022). The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers
MDPI., 14(22), 4834.
https://doi.org/10.3390/polym14224834
VL  - 14
IS  - 22
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5740
ER  - 

@misc{
author = "Stanišić, Marija D. and Popović Kokar, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Ognjanović, Miloš and Đokić, Veljko R. and Prodanović, Radivoje and Todorović, Tamara",
year = "2022",
title = "Primary research data for the article: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T. R.. (2022). The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers
MDPI., 14(22), 4834.
https://doi.org/10.3390/polym14224834",
volume = "14",
number = "22",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5740"
}

Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2022). Primary research data for the article: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T. R.. (2022). The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers
MDPI., 14(22), 4834.
https://doi.org/10.3390/polym14224834. , 14(22).
https://hdl.handle.net/21.15107/rcub_cherry_5740

Stanišić MD, Popović Kokar N, Ristić P, Balaž AM, Ognjanović M, Đokić VR, Prodanović R, Todorović T. Primary research data for the article: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T. R.. (2022). The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers
MDPI., 14(22), 4834.
https://doi.org/10.3390/polym14224834. 2022;14(22).
https://hdl.handle.net/21.15107/rcub_cherry_5740 .

Stanišić, Marija D., Popović Kokar, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Ognjanović, Miloš, Đokić, Veljko R., Prodanović, Radivoje, Todorović, Tamara, "Primary research data for the article: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T. R.. (2022). The Influence of Isoenzyme Composition and Chemical Modification on Horseradish Peroxidase@ZIF-8 Biocomposite Performance. in Polymers
MDPI., 14(22), 4834.
https://doi.org/10.3390/polym14224834", 14, no. 22 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5740 .

TY  - CONF
AU  - Stanišić, Marija D.
AU  - Ristić, Predrag
AU  - Đokić, Veljko
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5752
AB  - Metal-organic frameworks (MOFs) are a class of materials well-known for their high degree of crystallinity and
ultrahigh porosity. Modular synthesis from organic linkers and metal nodes allows for precise control of structure,
pore size and chemical functionality of MOFs. Recently, MOFs have been explored for their potential to form novel
biocomposites with proteins by a process termed biomimetic mineralization. These novel MOF biocomposites show
great promise for application to industrial biocatalysis where strategies for enhancing enzyme stability are of
significant interest. The protective capacity and applications of biomimetically mineralized biomacromolecule zeolitic
imidazolate framework (ZIF-8) composites are likely dependent on the charge of the biomolecule and the topology
of the mineralized ZIF-8 coating. Herein, we identify conditions to reliably yield the porous periodate oxidized
horseradish peroxidase@ZIF-8 sodalite topology biocomposite in preference to other more dense phases.
C3  - 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece
T1  - Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite
SP  - 138
EP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5752
ER  - 

@conference{
author = "Stanišić, Marija D. and Ristić, Predrag and Đokić, Veljko and Balaž, Ana Marija and Prodanović, Radivoje and Todorović, Tamara",
year = "2022",
abstract = "Metal-organic frameworks (MOFs) are a class of materials well-known for their high degree of crystallinity and
ultrahigh porosity. Modular synthesis from organic linkers and metal nodes allows for precise control of structure,
pore size and chemical functionality of MOFs. Recently, MOFs have been explored for their potential to form novel
biocomposites with proteins by a process termed biomimetic mineralization. These novel MOF biocomposites show
great promise for application to industrial biocatalysis where strategies for enhancing enzyme stability are of
significant interest. The protective capacity and applications of biomimetically mineralized biomacromolecule zeolitic
imidazolate framework (ZIF-8) composites are likely dependent on the charge of the biomolecule and the topology
of the mineralized ZIF-8 coating. Herein, we identify conditions to reliably yield the porous periodate oxidized
horseradish peroxidase@ZIF-8 sodalite topology biocomposite in preference to other more dense phases.",
journal = "19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece",
title = "Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite",
pages = "138-138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5752"
}

Stanišić, M. D., Ristić, P., Đokić, V., Balaž, A. M., Prodanović, R.,& Todorović, T.. (2022). Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite. in 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece, 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5752

Stanišić MD, Ristić P, Đokić V, Balaž AM, Prodanović R, Todorović T. Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite. in 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5752 .

Stanišić, Marija D., Ristić, Predrag, Đokić, Veljko, Balaž, Ana Marija, Prodanović, Radivoje, Todorović, Tamara, "Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite" in 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5752 .

TY  - GEN
AU  - Todorović, Tamara
AU  - Prodanović, Radivoje
AU  - Senćanski, Milan
AU  - Balaž, Ana Marija
AU  - Ristić, Predrag
AU  - Stanišić, Marija D.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5755
T2  - Seminar za studente, Beograd, 28. maj 2022.
T1  - Materijal za studente sa seminara projekta SYMBIOSIS
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5755
ER  - 

@misc{
author = "Todorović, Tamara and Prodanović, Radivoje and Senćanski, Milan and Balaž, Ana Marija and Ristić, Predrag and Stanišić, Marija D.",
year = "2022",
journal = "Seminar za studente, Beograd, 28. maj 2022.",
title = "Materijal za studente sa seminara projekta SYMBIOSIS",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5755"
}

Todorović, T., Prodanović, R., Senćanski, M., Balaž, A. M., Ristić, P.,& Stanišić, M. D.. (2022). Materijal za studente sa seminara projekta SYMBIOSIS. in Seminar za studente, Beograd, 28. maj 2022..
https://hdl.handle.net/21.15107/rcub_cherry_5755

Todorović T, Prodanović R, Senćanski M, Balaž AM, Ristić P, Stanišić MD. Materijal za studente sa seminara projekta SYMBIOSIS. in Seminar za studente, Beograd, 28. maj 2022.. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5755 .

Todorović, Tamara, Prodanović, Radivoje, Senćanski, Milan, Balaž, Ana Marija, Ristić, Predrag, Stanišić, Marija D., "Materijal za studente sa seminara projekta SYMBIOSIS" in Seminar za studente, Beograd, 28. maj 2022. (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5755 .

TY  - GEN
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5756
T2  - Projekat SYMBIOSIS
T1  - Promo-materijal projekta SYMBIOSIS
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5756
ER  - 

@misc{
author = "Todorović, Tamara",
year = "2022",
journal = "Projekat SYMBIOSIS",
title = "Promo-materijal projekta SYMBIOSIS",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5756"
}

Todorović, T.. (2022). Promo-materijal projekta SYMBIOSIS. in Projekat SYMBIOSIS.
https://hdl.handle.net/21.15107/rcub_cherry_5756

Todorović T. Promo-materijal projekta SYMBIOSIS. in Projekat SYMBIOSIS. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5756 .

Todorović, Tamara, "Promo-materijal projekta SYMBIOSIS" in Projekat SYMBIOSIS (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5756 .

TY  - THES
AU  - Stanojević, Nataša
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4722
AB  - Cilj ovog rada je kloniranje i ekspresija izoforme C1A peroksidaze iz rena u E. coli Shuffle
soju. Nakon ekspresije, bakterijska kultura je centrifugirana, ćelije lizirane i postavljene na
dijalizu naspram vode i pufera. Enzim je prečišćen afinitetnom hromatografijom sa
imobilizovanim metalom. Određen je stepen prečišćenja, koncentracija i aktivnost dobijenog
proizvoda. Nakon toga su ispitani kinetički parametri, kao i pH optimum, temperaturna
stabilnost i temperaturni optimum.
T1  - Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u Escherichia coli Shuffle soju
SP  - 6
EP  - 45
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4722
ER  - 

@misc{
author = "Stanojević, Nataša",
year = "2021",
abstract = "Cilj ovog rada je kloniranje i ekspresija izoforme C1A peroksidaze iz rena u E. coli Shuffle
soju. Nakon ekspresije, bakterijska kultura je centrifugirana, ćelije lizirane i postavljene na
dijalizu naspram vode i pufera. Enzim je prečišćen afinitetnom hromatografijom sa
imobilizovanim metalom. Određen je stepen prečišćenja, koncentracija i aktivnost dobijenog
proizvoda. Nakon toga su ispitani kinetički parametri, kao i pH optimum, temperaturna
stabilnost i temperaturni optimum.",
title = "Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u Escherichia coli Shuffle soju",
pages = "6-45",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4722"
}

Stanojević, N.. (2021). Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u Escherichia coli Shuffle soju. , 6-45.
https://hdl.handle.net/21.15107/rcub_cherry_4722

Stanojević N. Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u Escherichia coli Shuffle soju. 2021;:6-45.
https://hdl.handle.net/21.15107/rcub_cherry_4722 .

Stanojević, Nataša, "Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u Escherichia coli Shuffle soju" (2021):6-45,
https://hdl.handle.net/21.15107/rcub_cherry_4722 .

TY  - JOUR
AU  - Stanišić, Marija D.
AU  - Popović Kokar, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Senćanski, Milan
AU  - Ognjanović, Miloš
AU  - Đokić, Veljko R.
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4782
AB  - Zeolitic imidazolate framework-8 (ZIF-8) is widely used as a protective coating to encapsulate proteins via biomimetic mineralization. The formation of nucleation centers and further biocomposite crystal growth is entirely governed by the pure electrostatic interactions between the protein’s surface and the positively charged Zn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modification of surface amino acid residues can lead to a rapid biocomposite crystal formation. However, a chemical modification of carbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the present study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidation of GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule, from −10.2 to −36.9 mV, as shown by zeta potential measurements and native PAGE electrophoresis. Biomineralization experiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability of the ZIF-8 biocomposites. Periodate oxidation of carbohydrate components for glycoproteins can serve as a facile and general method for facilitating the biomimetic mineralization of other industrially relevant glycoproteins.
PB  - MDPI
T2  - Polymers
T1  - Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase
VL  - 13
IS  - 22
SP  - 3875
DO  - 10.3390/polym13223875
ER  - 

@article{
author = "Stanišić, Marija D. and Popović Kokar, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Senćanski, Milan and Ognjanović, Miloš and Đokić, Veljko R. and Prodanović, Radivoje and Todorović, Tamara",
year = "2021",
abstract = "Zeolitic imidazolate framework-8 (ZIF-8) is widely used as a protective coating to encapsulate proteins via biomimetic mineralization. The formation of nucleation centers and further biocomposite crystal growth is entirely governed by the pure electrostatic interactions between the protein’s surface and the positively charged Zn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modification of surface amino acid residues can lead to a rapid biocomposite crystal formation. However, a chemical modification of carbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the present study, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidation of GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule, from −10.2 to −36.9 mV, as shown by zeta potential measurements and native PAGE electrophoresis. Biomineralization experiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability of the ZIF-8 biocomposites. Periodate oxidation of carbohydrate components for glycoproteins can serve as a facile and general method for facilitating the biomimetic mineralization of other industrially relevant glycoproteins.",
publisher = "MDPI",
journal = "Polymers",
title = "Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase",
volume = "13",
number = "22",
pages = "3875",
doi = "10.3390/polym13223875"
}

Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers
MDPI., 13(22), 3875.
https://doi.org/10.3390/polym13223875

Stanišić MD, Popović Kokar N, Ristić P, Balaž AM, Senćanski M, Ognjanović M, Đokić VR, Prodanović R, Todorović T. Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers. 2021;13(22):3875.
doi:10.3390/polym13223875 .

Stanišić, Marija D., Popović Kokar, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Ognjanović, Miloš, Đokić, Veljko R., Prodanović, Radivoje, Todorović, Tamara, "Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase" in Polymers, 13, no. 22 (2021):3875,
https://doi.org/10.3390/polym13223875 . .

TY  - DATA
AU  - Stanišić, Marija D.
AU  - Popović Kokar, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Senćanski, Milan
AU  - Ognjanović, Miloš
AU  - Đokić, Veljko R.
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5741
T1  - Primary research data for: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers
MDPI., 13(22), 3875.
https://doi.org/10.3390/polym13223875
VL  - 13
IS  - 22
SP  - 3875
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5741
ER  - 

@misc{
author = "Stanišić, Marija D. and Popović Kokar, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Senćanski, Milan and Ognjanović, Miloš and Đokić, Veljko R. and Prodanović, Radivoje and Todorović, Tamara",
year = "2021",
title = "Primary research data for: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers
MDPI., 13(22), 3875.
https://doi.org/10.3390/polym13223875",
volume = "13",
number = "22",
pages = "3875",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5741"
}

Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Primary research data for: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers
MDPI., 13(22), 3875.
https://doi.org/10.3390/polym13223875. , 13(22), 3875.
https://hdl.handle.net/21.15107/rcub_cherry_5741

Stanišić MD, Popović Kokar N, Ristić P, Balaž AM, Senćanski M, Ognjanović M, Đokić VR, Prodanović R, Todorović T. Primary research data for: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers
MDPI., 13(22), 3875.
https://doi.org/10.3390/polym13223875. 2021;13(22):3875.
https://hdl.handle.net/21.15107/rcub_cherry_5741 .

Stanišić, Marija D., Popović Kokar, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Ognjanović, Miloš, Đokić, Veljko R., Prodanović, Radivoje, Todorović, Tamara, "Primary research data for: Stanišić, M. D., Popović Kokar, N., Ristić, P., Balaž, A. M., Senćanski, M., Ognjanović, M., Đokić, V. R., Prodanović, R.,& Todorović, T.. (2021). Chemical Modification of Glycoproteins’ Carbohydrate Moiety as a General Strategy for the Synthesis of Efficient Biocatalysts by Biomimetic Mineralization: The Case of Glucose Oxidase. in Polymers
MDPI., 13(22), 3875.
https://doi.org/10.3390/polym13223875", 13, no. 22 (2021):3875,
https://hdl.handle.net/21.15107/rcub_cherry_5741 .

TY  - CONF
AU  - Balaž, Ana Marija
AU  - Crnoglavac Popović, Milica
AU  - Stanišić, Marija D.
AU  - Ristić, Predrag
AU  - Senćanski, Milan
AU  - Todorović, Tamara
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5747
AB  - Enzyme immobilization enables maintenance of enzyme activity and structural stability even in adverse conditions 1. Structural changes in enzymes that can occur due to the action of organic solvents, inhibitors or increased temperature can be prevented by immobilization of the enzymes in metal–organic frameworks (MOFs). It is reported that several enzymes, such as cytochrome c and horseradish peroxidase (HRP) have been successfully incorporated into MOFs 2. The aim of this work is to produce wild type horseradish peroxidase, isoform C1A, and several mutants specially designed to increase the activity and stability of HRP while immobilized within selected MOFs. Wild type and its variants were produced in metalotrophic yeast, Pichia pastoris KM71H strain, their activity and basic kinetic parameters were determined and compared prior imobilization.
C3  - Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac
T1  - Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain
SP  - 49
EP  - 49
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5747
ER  - 

@conference{
author = "Balaž, Ana Marija and Crnoglavac Popović, Milica and Stanišić, Marija D. and Ristić, Predrag and Senćanski, Milan and Todorović, Tamara and Prodanović, Radivoje",
year = "2021",
abstract = "Enzyme immobilization enables maintenance of enzyme activity and structural stability even in adverse conditions 1. Structural changes in enzymes that can occur due to the action of organic solvents, inhibitors or increased temperature can be prevented by immobilization of the enzymes in metal–organic frameworks (MOFs). It is reported that several enzymes, such as cytochrome c and horseradish peroxidase (HRP) have been successfully incorporated into MOFs 2. The aim of this work is to produce wild type horseradish peroxidase, isoform C1A, and several mutants specially designed to increase the activity and stability of HRP while immobilized within selected MOFs. Wild type and its variants were produced in metalotrophic yeast, Pichia pastoris KM71H strain, their activity and basic kinetic parameters were determined and compared prior imobilization.",
journal = "Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac",
title = "Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain",
pages = "49-49",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5747"
}

Balaž, A. M., Crnoglavac Popović, M., Stanišić, M. D., Ristić, P., Senćanski, M., Todorović, T.,& Prodanović, R.. (2021). Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, 49-49.
https://hdl.handle.net/21.15107/rcub_cherry_5747

Balaž AM, Crnoglavac Popović M, Stanišić MD, Ristić P, Senćanski M, Todorović T, Prodanović R. Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac. 2021;:49-49.
https://hdl.handle.net/21.15107/rcub_cherry_5747 .

Balaž, Ana Marija, Crnoglavac Popović, Milica, Stanišić, Marija D., Ristić, Predrag, Senćanski, Milan, Todorović, Tamara, Prodanović, Radivoje, "Horseradish peroxidase C1A wild type gene and its variants expressed in Pichia pastoris KM71H strain" in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac (2021):49-49,
https://hdl.handle.net/21.15107/rcub_cherry_5747 .

TY  - CONF
AU  - Stanišić, Marija D.
AU  - Popović, Nikolina
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Senćanski, Milan
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5748
AB  - Glucose oxidase (GOx) is an enzyme that belongs to a group of oxidoreductases. This enzyme catalyzes the oxidation of glucose to gluconic acid using molecular oxygen as an electron acceptor. Glucose oxidase contains carbohydrates in its structure, most often mannose and glucose (11-13%) 1. Durability of GOx in harsh conditions can be enhanced by encapsulation within metal–organic frameworks via a process called biomimetic mineralisation. We demonstrate that chemical modification of carbohydrate parts on the protein surface by periodate oxidation is an effective method for control of biomimetic mineralisation by zeolitic imidazolate framework-8 (ZIF-8). Obtained GOx-ZIF-8 biocomposite had the higher half-life at 65oC, and higher specific activity than native GOx.
PB  - Beograd : Biohemijsko društvo Srbije
C3  - Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts
T1  - Biomimetic mineralisation of periodate oxidized glucose oxidase
SP  - 148
EP  - 148
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5748
ER  - 

@conference{
author = "Stanišić, Marija D. and Popović, Nikolina and Ristić, Predrag and Balaž, Ana Marija and Senćanski, Milan and Prodanović, Radivoje and Todorović, Tamara",
year = "2021",
abstract = "Glucose oxidase (GOx) is an enzyme that belongs to a group of oxidoreductases. This enzyme catalyzes the oxidation of glucose to gluconic acid using molecular oxygen as an electron acceptor. Glucose oxidase contains carbohydrates in its structure, most often mannose and glucose (11-13%) 1. Durability of GOx in harsh conditions can be enhanced by encapsulation within metal–organic frameworks via a process called biomimetic mineralisation. We demonstrate that chemical modification of carbohydrate parts on the protein surface by periodate oxidation is an effective method for control of biomimetic mineralisation by zeolitic imidazolate framework-8 (ZIF-8). Obtained GOx-ZIF-8 biocomposite had the higher half-life at 65oC, and higher specific activity than native GOx.",
publisher = "Beograd : Biohemijsko društvo Srbije",
journal = "Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts",
title = "Biomimetic mineralisation of periodate oxidized glucose oxidase",
pages = "148-148",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5748"
}

Stanišić, M. D., Popović, N., Ristić, P., Balaž, A. M., Senćanski, M., Prodanović, R.,& Todorović, T.. (2021). Biomimetic mineralisation of periodate oxidized glucose oxidase. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts
Beograd : Biohemijsko društvo Srbije., 148-148.
https://hdl.handle.net/21.15107/rcub_cherry_5748

Stanišić MD, Popović N, Ristić P, Balaž AM, Senćanski M, Prodanović R, Todorović T. Biomimetic mineralisation of periodate oxidized glucose oxidase. in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts. 2021;:148-148.
https://hdl.handle.net/21.15107/rcub_cherry_5748 .

Stanišić, Marija D., Popović, Nikolina, Ristić, Predrag, Balaž, Ana Marija, Senćanski, Milan, Prodanović, Radivoje, Todorović, Tamara, "Biomimetic mineralisation of periodate oxidized glucose oxidase" in Tenth Conference of Serbian Biochemical Society, 24 September 2021, Kragujevac, Book of Abstracts (2021):148-148,
https://hdl.handle.net/21.15107/rcub_cherry_5748 .

TY  - CONF
AU  - Senćanski, Milan
AU  - Prodanović, Radivoje
AU  - Ristić, Predrag
AU  - Balaž, Ana Marija
AU  - Stanišić, Marija D.
AU  - Todorović, Tamara
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5749
AB  - Enzymes as industrial biocatalysts offer numerous advantages over traditional chemical processes
concerning sustainability and process efficiency. Immobilization of enzymes on solid supporters is
one of the key strategies for improving the practical performances of enzymes.
Metal-organic frameworks (MOFs) are promising candidates for enzyme immobilization. MOFs are
porous coordination polymers consisting of metal-containing nodes and organic ligands linked
through coordination bonds. It has been demonstrated that proteins can be successfully immobilized
even in MOF pores whose apertures are smaller than the molecular dimension of the protein due to its
conformational flexibility.
For our study, we selected horseradish peroxidase (HRP) encapsulated in MOF PCN-888(Al). We
report the modelling of PCN-888(Al) MOF and the design of novel HRP mutants, which determine
their enzymatic activity and magnitude of intermolecular interactions with MOF. Using a combined
in silico approach, consisting of Informational Spectrum Method (ISM) bioinformatics method,
molecular docking and molecular dynamics simulations, we propose new HRP mutants, which show
higher/lower specific catalytic activity and higher/lower MOF-HRP dissociation constant, compared
to the wild type of enzyme.
PB  - Materials Research Society of Serbia
C3  - Twenty-Second Annual Conference YUCOMAT 2021, Herceg Novi, Montenegro, August 30 - September 3, 2021
T1  - Modelling of catalytic activity and enzyme-MOF interactions using combined in silico approach
SP  - 124
EP  - 124
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5749
ER  - 

@conference{
author = "Senćanski, Milan and Prodanović, Radivoje and Ristić, Predrag and Balaž, Ana Marija and Stanišić, Marija D. and Todorović, Tamara",
year = "2021",
abstract = "Enzymes as industrial biocatalysts offer numerous advantages over traditional chemical processes
concerning sustainability and process efficiency. Immobilization of enzymes on solid supporters is
one of the key strategies for improving the practical performances of enzymes.
Metal-organic frameworks (MOFs) are promising candidates for enzyme immobilization. MOFs are
porous coordination polymers consisting of metal-containing nodes and organic ligands linked
through coordination bonds. It has been demonstrated that proteins can be successfully immobilized
even in MOF pores whose apertures are smaller than the molecular dimension of the protein due to its
conformational flexibility.
For our study, we selected horseradish peroxidase (HRP) encapsulated in MOF PCN-888(Al). We
report the modelling of PCN-888(Al) MOF and the design of novel HRP mutants, which determine
their enzymatic activity and magnitude of intermolecular interactions with MOF. Using a combined
in silico approach, consisting of Informational Spectrum Method (ISM) bioinformatics method,
molecular docking and molecular dynamics simulations, we propose new HRP mutants, which show
higher/lower specific catalytic activity and higher/lower MOF-HRP dissociation constant, compared
to the wild type of enzyme.",
publisher = "Materials Research Society of Serbia",
journal = "Twenty-Second Annual Conference YUCOMAT 2021, Herceg Novi, Montenegro, August 30 - September 3, 2021",
title = "Modelling of catalytic activity and enzyme-MOF interactions using combined in silico approach",
pages = "124-124",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5749"
}

Senćanski, M., Prodanović, R., Ristić, P., Balaž, A. M., Stanišić, M. D.,& Todorović, T.. (2021). Modelling of catalytic activity and enzyme-MOF interactions using combined in silico approach. in Twenty-Second Annual Conference YUCOMAT 2021, Herceg Novi, Montenegro, August 30 - September 3, 2021
Materials Research Society of Serbia., 124-124.
https://hdl.handle.net/21.15107/rcub_cherry_5749

Senćanski M, Prodanović R, Ristić P, Balaž AM, Stanišić MD, Todorović T. Modelling of catalytic activity and enzyme-MOF interactions using combined in silico approach. in Twenty-Second Annual Conference YUCOMAT 2021, Herceg Novi, Montenegro, August 30 - September 3, 2021. 2021;:124-124.
https://hdl.handle.net/21.15107/rcub_cherry_5749 .

Senćanski, Milan, Prodanović, Radivoje, Ristić, Predrag, Balaž, Ana Marija, Stanišić, Marija D., Todorović, Tamara, "Modelling of catalytic activity and enzyme-MOF interactions using combined in silico approach" in Twenty-Second Annual Conference YUCOMAT 2021, Herceg Novi, Montenegro, August 30 - September 3, 2021 (2021):124-124,
https://hdl.handle.net/21.15107/rcub_cherry_5749 .

TY  - CONF
AU  - Ristić, Predrag
AU  - Pavlović, Pavle
AU  - Stanišić, Marija D.
AU  - Prodanović, Radivoje
AU  - Ognjanović, Miloš
AU  - Đokić, Veljko
AU  - Todorović, Tamara
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5750
AB  - Metal-organic frameworks (MOFs) are a class of inorganic materials with potential application in gas adsorption, biosensitization, biocatalysis, and drug delivery [1]. Zeolitic imidazolate frame-works (ZIFs) are a subclass of MOFs, particularly suitable for enzyme immobilization by biomi-metic mineralization [1]. ZIF-8 consisting of tetrahedral Zn(II) ions bridged via 2-methylimidazole ligands (mIM) is most commonly used for this purpose. However, the topology and morphology of ZIF-8 crystals vary depending on the experimental synthesis conditions. In addition, during the process of biomimetic mineralization, the biocomposite composed of the enzyme immobilized in ZIF-8 is washed with buffers and detergents to remove excess of an adsorbed enzyme, which can lead to the chemical transformation of the surface and undesirable release of the enzyme. There-fore, the influence of anion nature on the topology and morphology of ZIF-8 was investigated in this work, and the stability of ZIF-8 crystallites was tested in acetate buffer (0.1 M; pH = 5.5) and sodium dodecyl sulfate solution (ω = 10%). Crystal morphology was monitored by scanning elec-tron microscopy, while topology was determined using powder X-ray diffraction.
PB  - Beograd : Srpsko kristalografsko društvo
C3  - XXVII Konferencija Srpskog kristalografskog društva, 16-17. Septembar 2021, Kragujevac
T1  - Uticaj anjona, pufera i detergenata na topologiju i morfologiju ZIF-8 kristalita
SP  - 64
EP  - 65
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5750
ER  - 

@conference{
author = "Ristić, Predrag and Pavlović, Pavle and Stanišić, Marija D. and Prodanović, Radivoje and Ognjanović, Miloš and Đokić, Veljko and Todorović, Tamara",
year = "2021",
abstract = "Metal-organic frameworks (MOFs) are a class of inorganic materials with potential application in gas adsorption, biosensitization, biocatalysis, and drug delivery [1]. Zeolitic imidazolate frame-works (ZIFs) are a subclass of MOFs, particularly suitable for enzyme immobilization by biomi-metic mineralization [1]. ZIF-8 consisting of tetrahedral Zn(II) ions bridged via 2-methylimidazole ligands (mIM) is most commonly used for this purpose. However, the topology and morphology of ZIF-8 crystals vary depending on the experimental synthesis conditions. In addition, during the process of biomimetic mineralization, the biocomposite composed of the enzyme immobilized in ZIF-8 is washed with buffers and detergents to remove excess of an adsorbed enzyme, which can lead to the chemical transformation of the surface and undesirable release of the enzyme. There-fore, the influence of anion nature on the topology and morphology of ZIF-8 was investigated in this work, and the stability of ZIF-8 crystallites was tested in acetate buffer (0.1 M; pH = 5.5) and sodium dodecyl sulfate solution (ω = 10%). Crystal morphology was monitored by scanning elec-tron microscopy, while topology was determined using powder X-ray diffraction.",
publisher = "Beograd : Srpsko kristalografsko društvo",
journal = "XXVII Konferencija Srpskog kristalografskog društva, 16-17. Septembar 2021, Kragujevac",
title = "Uticaj anjona, pufera i detergenata na topologiju i morfologiju ZIF-8 kristalita",
pages = "64-65",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5750"
}

Ristić, P., Pavlović, P., Stanišić, M. D., Prodanović, R., Ognjanović, M., Đokić, V.,& Todorović, T.. (2021). Uticaj anjona, pufera i detergenata na topologiju i morfologiju ZIF-8 kristalita. in XXVII Konferencija Srpskog kristalografskog društva, 16-17. Septembar 2021, Kragujevac
Beograd : Srpsko kristalografsko društvo., 64-65.
https://hdl.handle.net/21.15107/rcub_cherry_5750

Ristić P, Pavlović P, Stanišić MD, Prodanović R, Ognjanović M, Đokić V, Todorović T. Uticaj anjona, pufera i detergenata na topologiju i morfologiju ZIF-8 kristalita. in XXVII Konferencija Srpskog kristalografskog društva, 16-17. Septembar 2021, Kragujevac. 2021;:64-65.
https://hdl.handle.net/21.15107/rcub_cherry_5750 .

Ristić, Predrag, Pavlović, Pavle, Stanišić, Marija D., Prodanović, Radivoje, Ognjanović, Miloš, Đokić, Veljko, Todorović, Tamara, "Uticaj anjona, pufera i detergenata na topologiju i morfologiju ZIF-8 kristalita" in XXVII Konferencija Srpskog kristalografskog društva, 16-17. Septembar 2021, Kragujevac (2021):64-65,
https://hdl.handle.net/21.15107/rcub_cherry_5750 .

TY  - THES
AU  - Pavlović, Pavle Lj.
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4726
AB  - Metal-organske umrežene strukture (MOF-ovi) su klasa neorganskih materijala sa potencijalnom primenom u adsorpciji gasova, biosenzibilizaciji, biokatalizi i isporuci lekova. Zeolitske imidazolske umrežene strukture (ZIF-ovi) su potklasa MOF-ova posebno pogodna za imobilizaciju enzima metodom biomimetičke mineralizacije. U ovu svrhu se najčešće koristi ZIF-8 koji se sastoji tetraedarskih jona Zn(II) povezanih preko mostnih 2-metilimidazolskih liganada. MeĎutim, topologija i morfologija kristala ZIF-8 varira u zavisnosti od eksperimentalnih uslova sinteze. TakoĎe, tokom procesa biomimetičke mineralizacije, biokompozit sastavljen od enzima imobilizovanog u ZIF-8 se ispira puferima i detergentima radi uklanjanja viška adsorbovanog enzima, pri čemu može doći do hemijske transformacije površine i nepoželjnog otpuštanja enzima. Stoga je u ovom radu ispitivan uticaj prirode anjona na topologiju i morfologiju ZIF-8, a stabilnost kristalita ZIF-8 je testirana u acetatnom puferu i rastvoru natrijum-dodecilsulfata. Morfologija kristala je praćena skenirajućom elektronskom mikroskopijom, dok je topologija odreĎena primenom difrakcije X-zraka na uzorku praha.
T1  - Uticaj anjona, pufera i detergenta na topologiju i morfologiju zif-8 kristalita
SP  - 1
EP  - 32
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4726
ER  - 

@misc{
author = "Pavlović, Pavle Lj.",
year = "2021",
abstract = "Metal-organske umrežene strukture (MOF-ovi) su klasa neorganskih materijala sa potencijalnom primenom u adsorpciji gasova, biosenzibilizaciji, biokatalizi i isporuci lekova. Zeolitske imidazolske umrežene strukture (ZIF-ovi) su potklasa MOF-ova posebno pogodna za imobilizaciju enzima metodom biomimetičke mineralizacije. U ovu svrhu se najčešće koristi ZIF-8 koji se sastoji tetraedarskih jona Zn(II) povezanih preko mostnih 2-metilimidazolskih liganada. MeĎutim, topologija i morfologija kristala ZIF-8 varira u zavisnosti od eksperimentalnih uslova sinteze. TakoĎe, tokom procesa biomimetičke mineralizacije, biokompozit sastavljen od enzima imobilizovanog u ZIF-8 se ispira puferima i detergentima radi uklanjanja viška adsorbovanog enzima, pri čemu može doći do hemijske transformacije površine i nepoželjnog otpuštanja enzima. Stoga je u ovom radu ispitivan uticaj prirode anjona na topologiju i morfologiju ZIF-8, a stabilnost kristalita ZIF-8 je testirana u acetatnom puferu i rastvoru natrijum-dodecilsulfata. Morfologija kristala je praćena skenirajućom elektronskom mikroskopijom, dok je topologija odreĎena primenom difrakcije X-zraka na uzorku praha.",
title = "Uticaj anjona, pufera i detergenta na topologiju i morfologiju zif-8 kristalita",
pages = "1-32",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4726"
}

Pavlović, P. Lj.. (2021). Uticaj anjona, pufera i detergenta na topologiju i morfologiju zif-8 kristalita. , 1-32.
https://hdl.handle.net/21.15107/rcub_cherry_4726

Pavlović PL. Uticaj anjona, pufera i detergenta na topologiju i morfologiju zif-8 kristalita. 2021;:1-32.
https://hdl.handle.net/21.15107/rcub_cherry_4726 .

Pavlović, Pavle Lj., "Uticaj anjona, pufera i detergenta na topologiju i morfologiju zif-8 kristalita" (2021):1-32,
https://hdl.handle.net/21.15107/rcub_cherry_4726 .

TY  - THES
AU  - Milić, Dejana
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4631
AB  - Cilj ovog rada je intracelularna produkcija lignin - peroksidaze iz Phanerochaete chrysosporium i odabir odgovarajućeg ekspresionog soja bakterije Escherichia coli, upotrebom pET-22b vektora. Takođe, ideja ovog master rada je uključivala i izolovanje enzima lignin – peroksidaze, kao i njegovo prečišćavanje za potrebe imobilizacije na metalo – organskim mrežama (MOF).
T1  - Heterologna ekspresija, izolovanje i prečišćavanje izoforme H8 lignin - peroksidaze iz Phanerochaete chrysosporium u Escherichia coli
SP  - 7
EP  - 65
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4631
ER  - 

@mastersthesis{
author = "Milić, Dejana",
year = "2021",
abstract = "Cilj ovog rada je intracelularna produkcija lignin - peroksidaze iz Phanerochaete chrysosporium i odabir odgovarajućeg ekspresionog soja bakterije Escherichia coli, upotrebom pET-22b vektora. Takođe, ideja ovog master rada je uključivala i izolovanje enzima lignin – peroksidaze, kao i njegovo prečišćavanje za potrebe imobilizacije na metalo – organskim mrežama (MOF).",
title = "Heterologna ekspresija, izolovanje i prečišćavanje izoforme H8 lignin - peroksidaze iz Phanerochaete chrysosporium u Escherichia coli",
pages = "7-65",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4631"
}

Milić, D.. (2021). Heterologna ekspresija, izolovanje i prečišćavanje izoforme H8 lignin - peroksidaze iz Phanerochaete chrysosporium u Escherichia coli. , 7-65.
https://hdl.handle.net/21.15107/rcub_cherry_4631

Milić D. Heterologna ekspresija, izolovanje i prečišćavanje izoforme H8 lignin - peroksidaze iz Phanerochaete chrysosporium u Escherichia coli. 2021;:7-65.
https://hdl.handle.net/21.15107/rcub_cherry_4631 .

Milić, Dejana, "Heterologna ekspresija, izolovanje i prečišćavanje izoforme H8 lignin - peroksidaze iz Phanerochaete chrysosporium u Escherichia coli" (2021):7-65,
https://hdl.handle.net/21.15107/rcub_cherry_4631 .

TY  - THES
AU  - Đajić, Milan
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4710
AB  - Peroksidaze predstavljaju grupu enzima koji učestvuju u oksido-redukcionim reakcijama koje uključuju vodonik peroksid. Peroksidaze su široko rasprostranjene u prirodi i mogu lako da se ekstrahuju iz većine biljnih tkiva i nekih životinjiskih. Jedan je od enzima koji je prvi otkriven, prvi podaci datiraju još iz 19-og vijeka. Podjeljene su u tri superfamilije prema porijeklu i načinu djelovanja na biljne perkosidaze, životinjske i katalaze.Peroksidaze su jedne od ključnih antioksidativnih enzima koji katalizuju oksidaciju različitih elektron donorskih supstrata uz razlaganje H2O2. Biljne peroksidaze su uključene u razne fiziološki značajne procese koji uključuju rast i razvoj biljke. Zahvaljujući njihovoj mogućnosti da katalizuju oksido-redukcione reakcije u prisustvu širokog spektra supstrata, smatraju se za jedne od najvažnijih enzima za primjenu u medicini, biohemiji, imunologiji, biotehonologiji i industriji.
T1  - Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u kvascu Pichia pastoris soj KM71H
SP  - 6
EP  - 46
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4710
ER  - 

@misc{
author = "Đajić, Milan",
year = "2021",
abstract = "Peroksidaze predstavljaju grupu enzima koji učestvuju u oksido-redukcionim reakcijama koje uključuju vodonik peroksid. Peroksidaze su široko rasprostranjene u prirodi i mogu lako da se ekstrahuju iz većine biljnih tkiva i nekih životinjiskih. Jedan je od enzima koji je prvi otkriven, prvi podaci datiraju još iz 19-og vijeka. Podjeljene su u tri superfamilije prema porijeklu i načinu djelovanja na biljne perkosidaze, životinjske i katalaze.Peroksidaze su jedne od ključnih antioksidativnih enzima koji katalizuju oksidaciju različitih elektron donorskih supstrata uz razlaganje H2O2. Biljne peroksidaze su uključene u razne fiziološki značajne procese koji uključuju rast i razvoj biljke. Zahvaljujući njihovoj mogućnosti da katalizuju oksido-redukcione reakcije u prisustvu širokog spektra supstrata, smatraju se za jedne od najvažnijih enzima za primjenu u medicini, biohemiji, imunologiji, biotehonologiji i industriji.",
title = "Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u kvascu Pichia pastoris soj KM71H",
pages = "6-46",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4710"
}

Đajić, M.. (2021). Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u kvascu Pichia pastoris soj KM71H. , 6-46.
https://hdl.handle.net/21.15107/rcub_cherry_4710

Đajić M. Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u kvascu Pichia pastoris soj KM71H. 2021;:6-46.
https://hdl.handle.net/21.15107/rcub_cherry_4710 .

Đajić, Milan, "Heterologna ekspresija, prečišćavanje i karakterizacija izoforme C1A peroksidaze iz rena u kvascu Pichia pastoris soj KM71H" (2021):6-46,
https://hdl.handle.net/21.15107/rcub_cherry_4710 .

TY  - THES
AU  - Vlajkov, Nikola M.
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4482
AB  - Cilj ovog rada je kloniranje i ekspresija izoforme H8 lignin peroksidaze u kvascu Pichia
pastoris soj KM71H. Dobijeni enzim je prečišćen upotrebom DEAE kolone, a potom detaljno
kinetički okarakterisan i definisani su mu pH optimum kao i temperaturna stabilnost.
T1  - Ekspresija, prečišćavanje i karakterizacija izoforme H8 lignin peroksidaze u kvascu Pichia pastoris
SP  - 1
EP  - 37
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4482
ER  - 

@misc{
author = "Vlajkov, Nikola M.",
year = "2021",
abstract = "Cilj ovog rada je kloniranje i ekspresija izoforme H8 lignin peroksidaze u kvascu Pichia
pastoris soj KM71H. Dobijeni enzim je prečišćen upotrebom DEAE kolone, a potom detaljno
kinetički okarakterisan i definisani su mu pH optimum kao i temperaturna stabilnost.",
title = "Ekspresija, prečišćavanje i karakterizacija izoforme H8 lignin peroksidaze u kvascu Pichia pastoris",
pages = "1-37",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4482"
}

Vlajkov, N. M.. (2021). Ekspresija, prečišćavanje i karakterizacija izoforme H8 lignin peroksidaze u kvascu Pichia pastoris. , 1-37.
https://hdl.handle.net/21.15107/rcub_cherry_4482

Vlajkov NM. Ekspresija, prečišćavanje i karakterizacija izoforme H8 lignin peroksidaze u kvascu Pichia pastoris. 2021;:1-37.
https://hdl.handle.net/21.15107/rcub_cherry_4482 .

Vlajkov, Nikola M., "Ekspresija, prečišćavanje i karakterizacija izoforme H8 lignin peroksidaze u kvascu Pichia pastoris" (2021):1-37,
https://hdl.handle.net/21.15107/rcub_cherry_4482 .