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 R.
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5269
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
IS  - 22
SP  - 4834
VL  - 14
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 R.",
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",
number = "22",
pages = "4834",
volume = "14",
doi = "10.3390/polym14224834"
}

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

Stanišić MD, Popović Kokar N, Ristić P, Balaž AM, Ognjanović M, Đokić VR, Prodanović R, Todorović TR. 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 R., "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 R.
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5951
T2  - Polymers
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 PolymersMDPI., 14(22), 4834.https://doi.org/10.3390/polym14224834
IS  - 22
VL  - 14
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 R.",
year = "2022",
journal = "Polymers",
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 PolymersMDPI., 14(22), 4834.https://doi.org/10.3390/polym14224834",
number = "22",
volume = "14",
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. R.. (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 PolymersMDPI., 14(22), 4834.https://doi.org/10.3390/polym14224834. in Polymers, 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 TR. 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 PolymersMDPI., 14(22), 4834.https://doi.org/10.3390/polym14224834. in Polymers. 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 R., "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 PolymersMDPI., 14(22), 4834.https://doi.org/10.3390/polym14224834" in Polymers, 14, no. 22 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5740 .

TY  - CONF
AU  - Stanišić, Marija
AU  - Ristić, Predrag
AU  - Đokić, Veljko
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5953
AB  - Metal-organic frameworks (MOFs) are a class of materials well-known for their high degree of crystallinity andultrahigh 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 novelbiocomposites with proteins by a process termed biomimetic mineralization. These novel MOF biocomposites showgreat promise for application to industrial biocatalysis where strategies for enhancing enzyme stability are ofsignificant interest. The protective capacity and applications of biomimetically mineralized biomacromolecule zeoliticimidazolate framework (ZIF-8) composites are likely dependent on the charge of the biomolecule and the topologyof the mineralized ZIF-8 coating. Herein, we identify conditions to reliably yield the porous periodate oxidizedhorseradish peroxidase@ZIF-8 sodalite topology biocomposite in preference to other more dense phases.
C3  - NANOTEXNOLOGY NN22, 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece
T1  - Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite
EP  - 138
SP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5752
ER  - 

@conference{
author = "Stanišić, Marija 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 andultrahigh 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 novelbiocomposites with proteins by a process termed biomimetic mineralization. These novel MOF biocomposites showgreat promise for application to industrial biocatalysis where strategies for enhancing enzyme stability are ofsignificant interest. The protective capacity and applications of biomimetically mineralized biomacromolecule zeoliticimidazolate framework (ZIF-8) composites are likely dependent on the charge of the biomolecule and the topologyof the mineralized ZIF-8 coating. Herein, we identify conditions to reliably yield the porous periodate oxidizedhorseradish peroxidase@ZIF-8 sodalite topology biocomposite in preference to other more dense phases.",
journal = "NANOTEXNOLOGY NN22, 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., Ristić, P., Đokić, V., Balaž, A. M., Prodanović, R.,& Todorović, T.. (2022). Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite. in NANOTEXNOLOGY NN22, 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece, 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5752

Stanišić M, Ristić P, Đokić V, Balaž AM, Prodanović R, Todorović T. Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite. in NANOTEXNOLOGY NN22, 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, Ristić, Predrag, Đokić, Veljko, Balaž, Ana Marija, Prodanović, Radivoje, Todorović, Tamara, "Periodate oxidized horseradish peroxidase@ZIF-8 nanocomposite" in NANOTEXNOLOGY NN22, 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  - Jakovetić, Sonja
AU  - Picazo-Espinosa, Rafael
AU  - Manzanera, Maximino
AU  - Stojanović, Željko
AU  - Prodanović, Radivoje
AU  - Miladinović, Ružica
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6096
AB  - Immobilization of lipase B from Candida antarctica was carried out using three different
immobilization methods, and two epoxy activated supports, comercial Eupergit C and
synthesized macroporous copolymer of glycidyl methacrylate (GMA) and ethylene glycol
dimethacrylate (EGDMA). The synthesized polymer was proven to be better for CALB
immobilization at both ionic strenghts that wrere applied, 0.1M and 1.25M. Investigation of
the effect of immobilization pH on the activity of immobilized enzymes, showed that the
highest activities were obtained when immobilization process was conducted in acidic
enviorments. The highest immobilized enzyme activity, 30.5 IU/ g of dry support, was
achieved when periodate method was employed. Glutaraldehyde activation of support did
not improve activity of obtained immobilized enzymes.
T1  - Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment
SP  - 129
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6096
ER  - 

@conference{
author = "Jakovetić, Sonja and Picazo-Espinosa, Rafael and Manzanera, Maximino and Stojanović, Željko and Prodanović, Radivoje and Miladinović, Ružica and Knežević-Jugović, Zorica",
year = "2012",
abstract = "Immobilization of lipase B from Candida antarctica was carried out using three different
immobilization methods, and two epoxy activated supports, comercial Eupergit C and
synthesized macroporous copolymer of glycidyl methacrylate (GMA) and ethylene glycol
dimethacrylate (EGDMA). The synthesized polymer was proven to be better for CALB
immobilization at both ionic strenghts that wrere applied, 0.1M and 1.25M. Investigation of
the effect of immobilization pH on the activity of immobilized enzymes, showed that the
highest activities were obtained when immobilization process was conducted in acidic
enviorments. The highest immobilized enzyme activity, 30.5 IU/ g of dry support, was
achieved when periodate method was employed. Glutaraldehyde activation of support did
not improve activity of obtained immobilized enzymes.",
title = "Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment",
pages = "129",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6096"
}

Jakovetić, S., Picazo-Espinosa, R., Manzanera, M., Stojanović, Ž., Prodanović, R., Miladinović, R.,& Knežević-Jugović, Z.. (2012). Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment. , 129.
https://hdl.handle.net/21.15107/rcub_technorep_6096

Jakovetić S, Picazo-Espinosa R, Manzanera M, Stojanović Ž, Prodanović R, Miladinović R, Knežević-Jugović Z. Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment. 2012;:129.
https://hdl.handle.net/21.15107/rcub_technorep_6096 .

Jakovetić, Sonja, Picazo-Espinosa, Rafael, Manzanera, Maximino, Stojanović, Željko, Prodanović, Radivoje, Miladinović, Ružica, Knežević-Jugović, Zorica, "Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment" (2012):129,
https://hdl.handle.net/21.15107/rcub_technorep_6096 .

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Milosavic, Nenad B.
AU  - Jovanović, Slobodan
AU  - Ćirković-Veličković, Tanja
AU  - Vujčić, Zoran
AU  - Jankov, Ratko M.
PY  - 2006
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5458
AB  - alpha-Glucosidase from baker's yeast was immobilized on macroporous copolymers of ethylene glycol dimethacrylate and glycidyl methacrylate, poly(GMA-co-EGDMA), with various surface characteristics and pore sizes ranging from 44 nm to 270 nm. Immobilization was done by glutaraldehyde on the copolymer previously modified with 1,2-diaminoethane. The specific activity of the obtained immobilized enzyme varied from 27 to 81 U/g depending on the employed copolymer. The half lives of the immobilized enzyme in cosolvents were influenced by the surface characteristics of the copolymer, ranging from 60 to 150 min in 35 % methanol and from 10 to 44 min in 45 % dimethyl sulphoxide (DMSO). The best stabilities were obtained when the enzyme was immobilized onto a copolymer having a pore size of 48 rim in methanol and 270 nm in DMSO.
AB  - α-Glukozidaza izolovana iz pekarskog kvasca je imobilizovana na makroporoznim glicidil-metakrilatima različitih površinskih karakteristika i veličina pora od 44 do 270 nm. Imobilizacija je izvedena glutaraldehidom na polimeru prethodno modifikovanom sa 1,2-diaminoetanom. Specifična aktivnost dobijenog imobilizovanog enzima je varirala od 27 do 81U/g u zavisnosti od vrste korišćenog polimera. Poluživoti imobilizovanog enzima u korastvaračima su zavisili od površinskih karakteristika polimera i kretali su se u opsegu od 60 do 150 min u 35%(v/v) metanolu i od 10 do 44 min u 45 % (v/v) dimetilsufoksidu. Najveća stabilnost u metanolu je dobijena imobilizacijom enzima na polimeru sa veličinom pora od 48 nm a u dimetilsulfoksidu na polimeru sa veličinom pora od 270 nm.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics
T1  - Stabilizacija α-glukozidaze u organskim rastvaračima imobilizacijom na makroporoznim (poli) glicidil metakrilatima različitih površinskih karakteristika
EP  - 347
IS  - 4
SP  - 339
VL  - 71
DO  - 10.2298/JSC0604339P
ER  - 

@article{
author = "Prodanović, Radivoje and Milosavic, Nenad B. and Jovanović, Slobodan and Ćirković-Veličković, Tanja and Vujčić, Zoran and Jankov, Ratko M.",
year = "2006",
abstract = "alpha-Glucosidase from baker's yeast was immobilized on macroporous copolymers of ethylene glycol dimethacrylate and glycidyl methacrylate, poly(GMA-co-EGDMA), with various surface characteristics and pore sizes ranging from 44 nm to 270 nm. Immobilization was done by glutaraldehyde on the copolymer previously modified with 1,2-diaminoethane. The specific activity of the obtained immobilized enzyme varied from 27 to 81 U/g depending on the employed copolymer. The half lives of the immobilized enzyme in cosolvents were influenced by the surface characteristics of the copolymer, ranging from 60 to 150 min in 35 % methanol and from 10 to 44 min in 45 % dimethyl sulphoxide (DMSO). The best stabilities were obtained when the enzyme was immobilized onto a copolymer having a pore size of 48 rim in methanol and 270 nm in DMSO., α-Glukozidaza izolovana iz pekarskog kvasca je imobilizovana na makroporoznim glicidil-metakrilatima različitih površinskih karakteristika i veličina pora od 44 do 270 nm. Imobilizacija je izvedena glutaraldehidom na polimeru prethodno modifikovanom sa 1,2-diaminoetanom. Specifična aktivnost dobijenog imobilizovanog enzima je varirala od 27 do 81U/g u zavisnosti od vrste korišćenog polimera. Poluživoti imobilizovanog enzima u korastvaračima su zavisili od površinskih karakteristika polimera i kretali su se u opsegu od 60 do 150 min u 35%(v/v) metanolu i od 10 do 44 min u 45 % (v/v) dimetilsufoksidu. Najveća stabilnost u metanolu je dobijena imobilizacijom enzima na polimeru sa veličinom pora od 48 nm a u dimetilsulfoksidu na polimeru sa veličinom pora od 270 nm.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics, Stabilizacija α-glukozidaze u organskim rastvaračima imobilizacijom na makroporoznim (poli) glicidil metakrilatima različitih površinskih karakteristika",
pages = "347-339",
number = "4",
volume = "71",
doi = "10.2298/JSC0604339P"
}

Prodanović, R., Milosavic, N. B., Jovanović, S., Ćirković-Veličković, T., Vujčić, Z.,& Jankov, R. M.. (2006). Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 71(4), 339-347.
https://doi.org/10.2298/JSC0604339P

Prodanović R, Milosavic NB, Jovanović S, Ćirković-Veličković T, Vujčić Z, Jankov RM. Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics. in Journal of the Serbian Chemical Society. 2006;71(4):339-347.
doi:10.2298/JSC0604339P .

Prodanović, Radivoje, Milosavic, Nenad B., Jovanović, Slobodan, Ćirković-Veličković, Tanja, Vujčić, Zoran, Jankov, Ratko M., "Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics" in Journal of the Serbian Chemical Society, 71, no. 4 (2006):339-347,
https://doi.org/10.2298/JSC0604339P . .

TY  - JOUR
AU  - Milosavic, N
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan
AU  - Novaković, Irena T.
AU  - Vujčić, Zoran
PY  - 2005
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5475
AB  - Amyloglucosidase from A. niger was covalently immobilized onto poly(GMA-co-EGDMA) by the glutaraldehyde and periodate method. The immobilization of amyloglucosidase after periodate oxidation gave a preparate with the highest specific activity reported so far on similar polymers. The obtained immobilized preparates show the same pH optimum, but a higher temperature optimum compared with the soluble enzyme. The kinetic parameters for the hydrolysis of soluble starch by free and both immobilized enzymes were determined.
AB  - Amiloglukozidaza iz A.niger je imobilizovana na poly(GMA-co-EGDMA) glutaraldehidnom i perjodatnom metodom. Imobilizacija amiloglukozidaze nakon perjodatne oksidacije daje preparat sa najvećom do sada objavljenom specifičnom aktivnosti na sličnim polimerima. Dobijeni imobilizovani preparat ima isti pH optimum ali povećani termooptimum u poređenju sa rastvornim enzimom. Određeni su i kinetički parametri za hidrolizu rastvornog skroba imobilizovanim kao i rastvornim enzimom.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and characterization of two types of covalently immobilized amyloglucosidase
T1  - Dobijanje i karakterizacija dva tipa imobilizovane amiloglukozidaze
EP  - 719
IS  - 5
SP  - 713
VL  - 70
DO  - 10.2298/JSC0505713M
ER  - 

@article{
author = "Milosavic, N and Prodanović, Radivoje and Jovanović, Slobodan and Novaković, Irena T. and Vujčić, Zoran",
year = "2005",
abstract = "Amyloglucosidase from A. niger was covalently immobilized onto poly(GMA-co-EGDMA) by the glutaraldehyde and periodate method. The immobilization of amyloglucosidase after periodate oxidation gave a preparate with the highest specific activity reported so far on similar polymers. The obtained immobilized preparates show the same pH optimum, but a higher temperature optimum compared with the soluble enzyme. The kinetic parameters for the hydrolysis of soluble starch by free and both immobilized enzymes were determined., Amiloglukozidaza iz A.niger je imobilizovana na poly(GMA-co-EGDMA) glutaraldehidnom i perjodatnom metodom. Imobilizacija amiloglukozidaze nakon perjodatne oksidacije daje preparat sa najvećom do sada objavljenom specifičnom aktivnosti na sličnim polimerima. Dobijeni imobilizovani preparat ima isti pH optimum ali povećani termooptimum u poređenju sa rastvornim enzimom. Određeni su i kinetički parametri za hidrolizu rastvornog skroba imobilizovanim kao i rastvornim enzimom.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and characterization of two types of covalently immobilized amyloglucosidase, Dobijanje i karakterizacija dva tipa imobilizovane amiloglukozidaze",
pages = "719-713",
number = "5",
volume = "70",
doi = "10.2298/JSC0505713M"
}

Milosavic, N., Prodanović, R., Jovanović, S., Novaković, I. T.,& Vujčić, Z.. (2005). Preparation and characterization of two types of covalently immobilized amyloglucosidase. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 70(5), 713-719.
https://doi.org/10.2298/JSC0505713M

Milosavic N, Prodanović R, Jovanović S, Novaković IT, Vujčić Z. Preparation and characterization of two types of covalently immobilized amyloglucosidase. in Journal of the Serbian Chemical Society. 2005;70(5):713-719.
doi:10.2298/JSC0505713M .

Milosavic, N, Prodanović, Radivoje, Jovanović, Slobodan, Novaković, Irena T., Vujčić, Zoran, "Preparation and characterization of two types of covalently immobilized amyloglucosidase" in Journal of the Serbian Chemical Society, 70, no. 5 (2005):713-719,
https://doi.org/10.2298/JSC0505713M . .

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan
AU  - Vujčić, Zoran
PY  - 2001
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5343
AB  - Invertase was immobilized via its carbohydrate moiety. The immobilized enzyme has a specific activity of 5500 IU g(-1), with 45% activity yield on immobilization. In a packed bed reactor, 90% 2.5 M sucrose was converted at a flow rate of 4 bed volumes h(-1). The obtained specific productivity at 40 degreesC of 3 kg l(-1) h(-1) is the best one so far. Long-term stability was 290 days in 2.5 M sucrose at 40 degreesC and at a flow rate of 3 bed volumes h(-1).
PB  - Kluwer Academic Publ, Dordrecht
T2  - Biotechnology Letters
T1  - Immobilization of invertase on a new type of macroporous glycidyl methacrylate
EP  - 1174
IS  - 14
SP  - 1171
VL  - 23
DO  - 10.1023/A:1010560911400
ER  - 

@article{
author = "Prodanović, Radivoje and Jovanović, Slobodan and Vujčić, Zoran",
year = "2001",
abstract = "Invertase was immobilized via its carbohydrate moiety. The immobilized enzyme has a specific activity of 5500 IU g(-1), with 45% activity yield on immobilization. In a packed bed reactor, 90% 2.5 M sucrose was converted at a flow rate of 4 bed volumes h(-1). The obtained specific productivity at 40 degreesC of 3 kg l(-1) h(-1) is the best one so far. Long-term stability was 290 days in 2.5 M sucrose at 40 degreesC and at a flow rate of 3 bed volumes h(-1).",
publisher = "Kluwer Academic Publ, Dordrecht",
journal = "Biotechnology Letters",
title = "Immobilization of invertase on a new type of macroporous glycidyl methacrylate",
pages = "1174-1171",
number = "14",
volume = "23",
doi = "10.1023/A:1010560911400"
}

Prodanović, R., Jovanović, S.,& Vujčić, Z.. (2001). Immobilization of invertase on a new type of macroporous glycidyl methacrylate. in Biotechnology Letters
Kluwer Academic Publ, Dordrecht., 23(14), 1171-1174.
https://doi.org/10.1023/A:1010560911400

Prodanović R, Jovanović S, Vujčić Z. Immobilization of invertase on a new type of macroporous glycidyl methacrylate. in Biotechnology Letters. 2001;23(14):1171-1174.
doi:10.1023/A:1010560911400 .

Prodanović, Radivoje, Jovanović, Slobodan, Vujčić, Zoran, "Immobilization of invertase on a new type of macroporous glycidyl methacrylate" in Biotechnology Letters, 23, no. 14 (2001):1171-1174,
https://doi.org/10.1023/A:1010560911400 . .