TY  - JOUR
AU  - Glišić, Sanja
AU  - Prodanović, Radivoje
AU  - Paessler, Slobodan
AU  - Perović, Vladimir
AU  - Milićević, Jelena
AU  - Prodanović, Olivera
AU  - Senčanski, Milan 
AU  - Kaličanin, Nevena
AU  - Protić, Sara
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5884
AB  - Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing can be an effective option for achieving a rapid response. This study used a combined in silico virtual screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking. Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro. After the expression and purification of PLpro, gramicidin D was screened for protease inhibition in vitro and was found to be active against PLpro. The current study’s findings are significant because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable safety profile.
PB  - MDPI
T2  - Int. J. Mol. Sci.
T1  - In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D
VL  - 24
IS  - 3
SP  - 1955
DO  - 10.3390/ijms24031955
ER  - 

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

Glišić, S., Prodanović, R., Paessler, S., Perović, V., Milićević, J., Prodanović, O., Senčanski, M., Kaličanin, N.,& Protić, S.. (2023). In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in Int. J. Mol. Sci.
MDPI., 24(3), 1955.
https://doi.org/10.3390/ijms24031955

Glišić S, Prodanović R, Paessler S, Perović V, Milićević J, Prodanović O, Senčanski M, Kaličanin N, Protić S. In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in Int. J. Mol. Sci.. 2023;24(3):1955.
doi:10.3390/ijms24031955 .

Glišić, Sanja, Prodanović, Radivoje, Paessler, Slobodan, Perović, Vladimir, Milićević, Jelena, Prodanović, Olivera, Senčanski, Milan , Kaličanin, Nevena, Protić, Sara, "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D" in Int. J. Mol. Sci., 24, no. 3 (2023):1955,
https://doi.org/10.3390/ijms24031955 . .

TY  - JOUR
AU  - Senćanski, Milan
AU  - Perović, Vladimir
AU  - Milićević, Jelena
AU  - Todorović, Tamara
AU  - Prodanović, Radivoje
AU  - Veljković, Veljko
AU  - Paessler, Slobodan
AU  - Glišić, Sanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5041
AB  - In the currentpandemic,findingan effectivedrugto preventortreatthe infectionis the highestpriority.A rapidand safeapproachto counteractCOVID-19is in silicodrugrepurposing.The SARS-CoV-2PLpropromotesviral replicationand modu-latesthe hostimmunesystem,resultingin inhibitionof thehostantiviralinnateimmuneresponse,and thereforeis anattractivedrugtarget.In this study,we useda combinedinsilicovirtualscreeningfor candidatesfor SARS-CoV-2PLproproteaseinhibitors.We usedthe Informationalspectrummethodappliedfor SmallMoleculesfor searchingthe Drugbankdatabasefollowedby moleculardocking.Afterin silicoscreen-ing of drugspace,we identified44 drugsas potentialSARS-CoV-2PLproinhibitorsthat we proposefor furtherexperimentaltesting.
PB  - Wiley-VCH
T2  - ChemistryOpen
T1  - Identification of SARS-CoV-2 Papain-like Protease (PLpro) Inhibitors Using Combined Computational Approach
VL  - 11
IS  - 2
SP  - e202100248
DO  - 10.1002/open.202100248
ER  - 

@article{
author = "Senćanski, Milan and Perović, Vladimir and Milićević, Jelena and Todorović, Tamara and Prodanović, Radivoje and Veljković, Veljko and Paessler, Slobodan and Glišić, Sanja",
year = "2022",
abstract = "In the currentpandemic,findingan effectivedrugto preventortreatthe infectionis the highestpriority.A rapidand safeapproachto counteractCOVID-19is in silicodrugrepurposing.The SARS-CoV-2PLpropromotesviral replicationand modu-latesthe hostimmunesystem,resultingin inhibitionof thehostantiviralinnateimmuneresponse,and thereforeis anattractivedrugtarget.In this study,we useda combinedinsilicovirtualscreeningfor candidatesfor SARS-CoV-2PLproproteaseinhibitors.We usedthe Informationalspectrummethodappliedfor SmallMoleculesfor searchingthe Drugbankdatabasefollowedby moleculardocking.Afterin silicoscreen-ing of drugspace,we identified44 drugsas potentialSARS-CoV-2PLproinhibitorsthat we proposefor furtherexperimentaltesting.",
publisher = "Wiley-VCH",
journal = "ChemistryOpen",
title = "Identification of SARS-CoV-2 Papain-like Protease (PLpro) Inhibitors Using Combined Computational Approach",
volume = "11",
number = "2",
pages = "e202100248",
doi = "10.1002/open.202100248"
}

Senćanski, M., Perović, V., Milićević, J., Todorović, T., Prodanović, R., Veljković, V., Paessler, S.,& Glišić, S.. (2022). Identification of SARS-CoV-2 Papain-like Protease (PLpro) Inhibitors Using Combined Computational Approach. in ChemistryOpen
Wiley-VCH., 11(2), e202100248.
https://doi.org/10.1002/open.202100248

Senćanski M, Perović V, Milićević J, Todorović T, Prodanović R, Veljković V, Paessler S, Glišić S. Identification of SARS-CoV-2 Papain-like Protease (PLpro) Inhibitors Using Combined Computational Approach. in ChemistryOpen. 2022;11(2):e202100248.
doi:10.1002/open.202100248 .

Senćanski, Milan, Perović, Vladimir, Milićević, Jelena, Todorović, Tamara, Prodanović, Radivoje, Veljković, Veljko, Paessler, Slobodan, Glišić, Sanja, "Identification of SARS-CoV-2 Papain-like Protease (PLpro) Inhibitors Using Combined Computational Approach" in ChemistryOpen, 11, no. 2 (2022):e202100248,
https://doi.org/10.1002/open.202100248 . .

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  - 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  - 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  - 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  - 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/123456789/5754
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 isoenzymes composition and chemical modification on horseradish peroxidase@ZIF-8 bio-composite performance
VL  - 14
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 isoenzymes composition and chemical modification on horseradish peroxidase@ZIF-8 bio-composite performance",
volume = "14",
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 isoenzymes composition and chemical modification on horseradish peroxidase@ZIF-8 bio-composite performance. in Polymers
MDPI., 14, 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 isoenzymes composition and chemical modification on horseradish peroxidase@ZIF-8 bio-composite performance. in Polymers. 2022;14:4834.
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 isoenzymes composition and chemical modification on horseradish peroxidase@ZIF-8 bio-composite performance" in Polymers, 14 (2022):4834,
https://doi.org/10.3390/polym14224834 . .

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  - JOUR
AU  - Filipović, Lidija
AU  - Spasojević, Milica
AU  - Prodanović, Radivoje
AU  - Korać, Aleksandra
AU  - Matijaševic, Suzana
AU  - Brajušković, Goran
AU  - de Marco, Ario
AU  - Popović, Milica M.
PY  - 2022
UR  - https://pubmed.ncbi.nlm.nih.gov/35301156/
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5152
AB  - Correct elucidation of physiological and pathological processes mediated by extracellular vesicles (EV) is highly dependent on the reliability of the method used for their purification. Currently available chemical/physical protocols for sample fractionation are time-consuming, often scarcely reproducible and their yields are low. Immuno-capture based approaches could represent an effective purification alternative to obtain homogeneous EV samples. An easy-to-operate chromatography system was set-up for the purification of intact EVs based on a single domain (VHH) antibodies-copolymer matrix suitable for biological samples as different as conditioned cell culture medium and human plasma. Methacrylate-based copolymer is a porous solid support, the chemical versatility of which enables its efficient functionalization with VHHs. The combined analyses of morphological features and biomarker (CD9, CD63 and CD81) presence indicated that the recovered EVs were exosomes. The lipoprotein markers APO-A1 and APO-B were both negative in tested samples. This is the first report demonstrating the successful application of spherical porous methacrylate-based copolymer coupled with VHHs for the exosome isolation from biological fluids. This inexpensive immunoaffinity method has the potential to be applied for the isolation of EVs belonging to different morphological and physiological classes.
PB  - Elsevier
T2  - New Biotechnology
T1  - Affinity-based isolation of extracellular vesicles by means of single-domain antibodies bound to macroporous methacrylate-based copolymer
VL  - 69
SP  - 36
EP  - 48
DO  - 10.1016/j.nbt.2022.03.001
ER  - 

@article{
author = "Filipović, Lidija and Spasojević, Milica and Prodanović, Radivoje and Korać, Aleksandra and Matijaševic, Suzana and Brajušković, Goran and de Marco, Ario and Popović, Milica M.",
year = "2022",
abstract = "Correct elucidation of physiological and pathological processes mediated by extracellular vesicles (EV) is highly dependent on the reliability of the method used for their purification. Currently available chemical/physical protocols for sample fractionation are time-consuming, often scarcely reproducible and their yields are low. Immuno-capture based approaches could represent an effective purification alternative to obtain homogeneous EV samples. An easy-to-operate chromatography system was set-up for the purification of intact EVs based on a single domain (VHH) antibodies-copolymer matrix suitable for biological samples as different as conditioned cell culture medium and human plasma. Methacrylate-based copolymer is a porous solid support, the chemical versatility of which enables its efficient functionalization with VHHs. The combined analyses of morphological features and biomarker (CD9, CD63 and CD81) presence indicated that the recovered EVs were exosomes. The lipoprotein markers APO-A1 and APO-B were both negative in tested samples. This is the first report demonstrating the successful application of spherical porous methacrylate-based copolymer coupled with VHHs for the exosome isolation from biological fluids. This inexpensive immunoaffinity method has the potential to be applied for the isolation of EVs belonging to different morphological and physiological classes.",
publisher = "Elsevier",
journal = "New Biotechnology",
title = "Affinity-based isolation of extracellular vesicles by means of single-domain antibodies bound to macroporous methacrylate-based copolymer",
volume = "69",
pages = "36-48",
doi = "10.1016/j.nbt.2022.03.001"
}

Filipović, L., Spasojević, M., Prodanović, R., Korać, A., Matijaševic, S., Brajušković, G., de Marco, A.,& Popović, M. M.. (2022). Affinity-based isolation of extracellular vesicles by means of single-domain antibodies bound to macroporous methacrylate-based copolymer. in New Biotechnology
Elsevier., 69, 36-48.
https://doi.org/10.1016/j.nbt.2022.03.001

Filipović L, Spasojević M, Prodanović R, Korać A, Matijaševic S, Brajušković G, de Marco A, Popović MM. Affinity-based isolation of extracellular vesicles by means of single-domain antibodies bound to macroporous methacrylate-based copolymer. in New Biotechnology. 2022;69:36-48.
doi:10.1016/j.nbt.2022.03.001 .

Filipović, Lidija, Spasojević, Milica, Prodanović, Radivoje, Korać, Aleksandra, Matijaševic, Suzana, Brajušković, Goran, de Marco, Ario, Popović, Milica M., "Affinity-based isolation of extracellular vesicles by means of single-domain antibodies bound to macroporous methacrylate-based copolymer" in New Biotechnology, 69 (2022):36-48,
https://doi.org/10.1016/j.nbt.2022.03.001 . .

TY  - DATA
AU  - Filipović, Lidija
AU  - Spasojević, Milica
AU  - Prodanović, Radivoje
AU  - Korać, Aleksandra
AU  - Matijaševic, Suzana
AU  - Brajušković, Goran
AU  - de Marco, Ario
AU  - Popović, Milica M.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5152
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5153
AB  - Correct elucidation of physiological and pathological processes mediated by extracellular vesicles (EV) is highly dependent on the reliability of the method used for their purification. Currently available chemical/physical protocols for sample fractionation are time-consuming, often scarcely reproducible and their yields are low. Immuno-capture based approaches could represent an effective purification alternative to obtain homogeneous EV samples. An easy-to-operate chromatography system was set-up for the purification of intact EVs based on a single domain (VHH) antibodies-copolymer matrix suitable for biological samples as different as conditioned cell culture medium and human plasma. Methacrylate-based copolymer is a porous solid support, the chemical versatility of which enables its efficient functionalization with VHHs. The combined analyses of morphological features and biomarker (CD9, CD63 and CD81) presence indicated that the recovered EVs were exosomes. The lipoprotein markers APO-A1 and APO-B were both negative in tested samples. This is the first report demonstrating the successful application of spherical porous methacrylate-based copolymer coupled with VHHs for the exosome isolation from biological fluids. This inexpensive immunoaffinity method has the potential to be applied for the isolation of EVs belonging to different morphological and physiological classes.
PB  - Elsevier
T2  - New Biotechnology
T1  - Supplementary information for the article: Filipović, L.; Spasojević, M.; Prodanović, R.; Korać, A.; Matijaševic, S.; Brajušković, G.; de Marco, A.; Popović, M. Affinity-Based Isolation of Extracellular Vesicles by Means of Single-Domain Antibodies Bound to Macroporous Methacrylate-Based Copolymer. New Biotechnology 2022, 69, 36–48. https://doi.org/10.1016/j.nbt.2022.03.001.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5153
ER  - 

@misc{
author = "Filipović, Lidija and Spasojević, Milica and Prodanović, Radivoje and Korać, Aleksandra and Matijaševic, Suzana and Brajušković, Goran and de Marco, Ario and Popović, Milica M.",
year = "2022",
abstract = "Correct elucidation of physiological and pathological processes mediated by extracellular vesicles (EV) is highly dependent on the reliability of the method used for their purification. Currently available chemical/physical protocols for sample fractionation are time-consuming, often scarcely reproducible and their yields are low. Immuno-capture based approaches could represent an effective purification alternative to obtain homogeneous EV samples. An easy-to-operate chromatography system was set-up for the purification of intact EVs based on a single domain (VHH) antibodies-copolymer matrix suitable for biological samples as different as conditioned cell culture medium and human plasma. Methacrylate-based copolymer is a porous solid support, the chemical versatility of which enables its efficient functionalization with VHHs. The combined analyses of morphological features and biomarker (CD9, CD63 and CD81) presence indicated that the recovered EVs were exosomes. The lipoprotein markers APO-A1 and APO-B were both negative in tested samples. This is the first report demonstrating the successful application of spherical porous methacrylate-based copolymer coupled with VHHs for the exosome isolation from biological fluids. This inexpensive immunoaffinity method has the potential to be applied for the isolation of EVs belonging to different morphological and physiological classes.",
publisher = "Elsevier",
journal = "New Biotechnology",
title = "Supplementary information for the article: Filipović, L.; Spasojević, M.; Prodanović, R.; Korać, A.; Matijaševic, S.; Brajušković, G.; de Marco, A.; Popović, M. Affinity-Based Isolation of Extracellular Vesicles by Means of Single-Domain Antibodies Bound to Macroporous Methacrylate-Based Copolymer. New Biotechnology 2022, 69, 36–48. https://doi.org/10.1016/j.nbt.2022.03.001.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5153"
}

Filipović, L., Spasojević, M., Prodanović, R., Korać, A., Matijaševic, S., Brajušković, G., de Marco, A.,& Popović, M. M.. (2022). Supplementary information for the article: Filipović, L.; Spasojević, M.; Prodanović, R.; Korać, A.; Matijaševic, S.; Brajušković, G.; de Marco, A.; Popović, M. Affinity-Based Isolation of Extracellular Vesicles by Means of Single-Domain Antibodies Bound to Macroporous Methacrylate-Based Copolymer. New Biotechnology 2022, 69, 36–48. https://doi.org/10.1016/j.nbt.2022.03.001.. in New Biotechnology
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_5153

Filipović L, Spasojević M, Prodanović R, Korać A, Matijaševic S, Brajušković G, de Marco A, Popović MM. Supplementary information for the article: Filipović, L.; Spasojević, M.; Prodanović, R.; Korać, A.; Matijaševic, S.; Brajušković, G.; de Marco, A.; Popović, M. Affinity-Based Isolation of Extracellular Vesicles by Means of Single-Domain Antibodies Bound to Macroporous Methacrylate-Based Copolymer. New Biotechnology 2022, 69, 36–48. https://doi.org/10.1016/j.nbt.2022.03.001.. in New Biotechnology. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5153 .

Filipović, Lidija, Spasojević, Milica, Prodanović, Radivoje, Korać, Aleksandra, Matijaševic, Suzana, Brajušković, Goran, de Marco, Ario, Popović, Milica M., "Supplementary information for the article: Filipović, L.; Spasojević, M.; Prodanović, R.; Korać, A.; Matijaševic, S.; Brajušković, G.; de Marco, A.; Popović, M. Affinity-Based Isolation of Extracellular Vesicles by Means of Single-Domain Antibodies Bound to Macroporous Methacrylate-Based Copolymer. New Biotechnology 2022, 69, 36–48. https://doi.org/10.1016/j.nbt.2022.03.001." in New Biotechnology (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5153 .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Spasojević, Milica
AU  - Stojanović, Željko
AU  - Veljović, Đorđe
AU  - Krstić, Jugoslav
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2022
UR  - https://link.springer.com/article/10.1007/s10924-021-02364-3
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5205
AB  - Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.
PB  - Springer
T2  - Journal of Polymers and the Environment
T1  - Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol
VL  - 30
SP  - 3005
EP  - 3020
DO  - 10.1007/s10924-021-02364-3
ER  - 

@article{
author = "Pantić, Nevena and Spasojević, Milica and Stojanović, Željko and Veljović, Đorđe and Krstić, Jugoslav and Balaž, Ana Marija and Prodanović, Radivoje and Prodanović, Olivera",
year = "2022",
abstract = "Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.",
publisher = "Springer",
journal = "Journal of Polymers and the Environment",
title = "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol",
volume = "30",
pages = "3005-3020",
doi = "10.1007/s10924-021-02364-3"
}

Pantić, N., Spasojević, M., Stojanović, Ž., Veljović, Đ., Krstić, J., Balaž, A. M., Prodanović, R.,& Prodanović, O.. (2022). Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment
Springer., 30, 3005-3020.
https://doi.org/10.1007/s10924-021-02364-3

Pantić N, Spasojević M, Stojanović Ž, Veljović Đ, Krstić J, Balaž AM, Prodanović R, Prodanović O. Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment. 2022;30:3005-3020.
doi:10.1007/s10924-021-02364-3 .

Pantić, Nevena, Spasojević, Milica, Stojanović, Željko, Veljović, Đorđe, Krstić, Jugoslav, Balaž, Ana Marija, Prodanović, Radivoje, Prodanović, Olivera, "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol" in Journal of Polymers and the Environment, 30 (2022):3005-3020,
https://doi.org/10.1007/s10924-021-02364-3 . .

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