TY  - CONF
AU  - Ristić, Predrag
AU  - Stanišić, Marija
AU  - Đokić, Veljko
AU  - Balaž, Ana Marija
AU  - Mitić, Dragana
AU  - Prodanović, Radivoje
AU  - Todorović, Tamara
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5952
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 aprotective coating to encapsulate proteins. The formation of nucleation centres and further biocomposite particlegrowth is entirely governed by the pure electrostatic interactions between the protein’s surface and positively chargedZn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modificationof surface amino acid residues can lead to a rapid biocomposite formation. However, a chemical modification ofcarbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the presentstudy, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidationof GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule. Biomineralizationexperiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability ofthe ZIF-8 biocomposites.
C3  - Book of abstracts - NANOTEXNOLOGY NN22, 19th International Conference on Nanosciences & Nanotechnologies, 5-8 July 2022, Thessaloniki, Greece
T1  - Periodate oxidized glucose oxidase@ZIF-8 nanocomposite
EP  - 138
SP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5753
ER  - 

@conference{
author = "Ristić, Predrag and Stanišić, Marija 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 aprotective coating to encapsulate proteins. The formation of nucleation centres and further biocomposite particlegrowth is entirely governed by the pure electrostatic interactions between the protein’s surface and positively chargedZn(II) metal ions. It was previously shown that enhancing these electrostatic interactions by a chemical modificationof surface amino acid residues can lead to a rapid biocomposite formation. However, a chemical modification ofcarbohydrate components by periodate oxidation for glycoproteins can serve as an alternative strategy. In the presentstudy, an industrially important enzyme glucose oxidase (GOx) was selected as a model system. Periodate oxidationof GOx by 2.5 mM sodium periodate increased negative charge on the enzyme molecule. Biomineralizationexperiments with oxidized GOx resulted in higher specific activity, effectiveness factor, and higher thermostability ofthe ZIF-8 biocomposites.",
journal = "Book of abstracts - NANOTEXNOLOGY NN22, 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., Đokić, V., Balaž, A. M., Mitić, D., Prodanović, R.,& Todorović, T.. (2022). Periodate oxidized glucose oxidase@ZIF-8 nanocomposite. in Book of abstracts - NANOTEXNOLOGY NN22, 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 M, Đokić V, Balaž AM, Mitić D, Prodanović R, Todorović T. Periodate oxidized glucose oxidase@ZIF-8 nanocomposite. in Book of abstracts - 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_5753 .

Ristić, Predrag, Stanišić, Marija, Đokić, Veljko, Balaž, Ana Marija, Mitić, Dragana, Prodanović, Radivoje, Todorović, Tamara, "Periodate oxidized glucose oxidase@ZIF-8 nanocomposite" in Book of abstracts - 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_5753 .

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  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5096
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
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",
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..
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;.
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 (2022),
https://doi.org/10.1007/s10924-021-02364-3 . .

TY  - CONF
AU  - Ristić, Predrag
AU  - Pavlović, Pavle
AU  - Stanišić, Marija
AU  - Prodanović, Radivoje
AU  - Ognjanović, Miloš
AU  - Đokić, Veljko
AU  - Todorović, Tamara
PY  - 2021
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5954
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
EP  - 65
SP  - 64
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5750
ER  - 

@conference{
author = "Ristić, Predrag and Pavlović, Pavle and Stanišić, Marija 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 = "65-64",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5750"
}

Ristić, P., Pavlović, P., Stanišić, M., 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 M, 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, 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  - JOUR
AU  - Prodanović, Olivera
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Knežević-Jugović, Zorica
AU  - Prodanović, Radivoje
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2187
AB  - A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.
PB  - Springer, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers
EP  - 1301
IS  - 5
SP  - 1288
VL  - 168
DO  - 10.1007/s12010-012-9857-7
ER  - 

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

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

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

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

TY  - JOUR
AU  - Ahmed, Khaled S.O.H.
AU  - Milosavić, Nenad
AU  - Popović, Milica M.
AU  - Prodanović, Radivoje
AU  - Knežević, Zorica
AU  - Jankov, Ratko
PY  - 2007
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1111
AB  - α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45 ºC for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase.
AB  - Maltaza iz S. cerevisiae je kovalentno imobilizovana na Sepabeads EC-EA nakon aktivacije nosača rastvorom glutaraldehida. Ispitivanjem kinetike imobilizacije utvrđeno je da se 25 % enzima imobilizuje nakon 24 časa. Imobilizovana α-glukozidaza ima isti pH optimum kao i rastvorni enzim, dok je optimalna temperatura za aktivnost imobilizovanog enzima uvećana za 10 °C u poređenju sa rastvornim enzimom. Kada se uporede zaostale aktivnosti rastvorne i imobilizovane forme α-glukozidaze, nakon inkubacije od 1 h na 45 °C rastvorni enzim ne pokazuje aktivnost dok imobilizovana forma zadržava oko 20 % početne aktivnosti. Imobilizovana forma enzima zadržava 20 % početne aktivnosti čak i posle 3 h inkubacije na 45 °C.
PB  - Serbian Chemical Society, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae
T1  - Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae
EP  - 1263
IS  - 12
SP  - 1255
VL  - 72
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1111
ER  - 

@article{
author = "Ahmed, Khaled S.O.H. and Milosavić, Nenad and Popović, Milica M. and Prodanović, Radivoje and Knežević, Zorica and Jankov, Ratko",
year = "2007",
abstract = "α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45 ºC for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase., Maltaza iz S. cerevisiae je kovalentno imobilizovana na Sepabeads EC-EA nakon aktivacije nosača rastvorom glutaraldehida. Ispitivanjem kinetike imobilizacije utvrđeno je da se 25 % enzima imobilizuje nakon 24 časa. Imobilizovana α-glukozidaza ima isti pH optimum kao i rastvorni enzim, dok je optimalna temperatura za aktivnost imobilizovanog enzima uvećana za 10 °C u poređenju sa rastvornim enzimom. Kada se uporede zaostale aktivnosti rastvorne i imobilizovane forme α-glukozidaze, nakon inkubacije od 1 h na 45 °C rastvorni enzim ne pokazuje aktivnost dok imobilizovana forma zadržava oko 20 % početne aktivnosti. Imobilizovana forma enzima zadržava 20 % početne aktivnosti čak i posle 3 h inkubacije na 45 °C.",
publisher = "Serbian Chemical Society, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae, Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae",
pages = "1263-1255",
number = "12",
volume = "72",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1111"
}

Ahmed, K. S.O.H., Milosavić, N., Popović, M. M., Prodanović, R., Knežević, Z.,& Jankov, R.. (2007). Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Serbian Chemical Society, Belgrade., 72(12), 1255-1263.
https://hdl.handle.net/21.15107/rcub_technorep_1111

Ahmed KS, Milosavić N, Popović MM, Prodanović R, Knežević Z, Jankov R. Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
https://hdl.handle.net/21.15107/rcub_technorep_1111 .

Ahmed, Khaled S.O.H., Milosavić, Nenad, Popović, Milica M., Prodanović, Radivoje, Knežević, Zorica, Jankov, Ratko, "Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://hdl.handle.net/21.15107/rcub_technorep_1111 .

TY  - JOUR
AU  - Knežević, Zorica
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Jakovljević, Živana
AU  - Prodanović, Radivoje
PY  - 2006
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/990
AB  - The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system.
PB  - Elsevier, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment
EP  - 278
IS  - 3
SP  - 269
VL  - 30
DO  - 10.1016/j.bej.2006.05.009
ER  - 

@article{
author = "Knežević, Zorica and Milosavić, Nenad and Bezbradica, Dejan and Jakovljević, Živana and Prodanović, Radivoje",
year = "2006",
abstract = "The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system.",
publisher = "Elsevier, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment",
pages = "278-269",
number = "3",
volume = "30",
doi = "10.1016/j.bej.2006.05.009"
}

Knežević, Z., Milosavić, N., Bezbradica, D., Jakovljević, Ž.,& Prodanović, R.. (2006). Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment. in Biochemical Engineering Journal
Elsevier, Amsterdam., 30(3), 269-278.
https://doi.org/10.1016/j.bej.2006.05.009

Knežević Z, Milosavić N, Bezbradica D, Jakovljević Ž, Prodanović R. Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment. in Biochemical Engineering Journal. 2006;30(3):269-278.
doi:10.1016/j.bej.2006.05.009 .

Knežević, Zorica, Milosavić, Nenad, Bezbradica, Dejan, Jakovljević, Živana, Prodanović, Radivoje, "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment" in Biochemical Engineering Journal, 30, no. 3 (2006):269-278,
https://doi.org/10.1016/j.bej.2006.05.009 . .

TY  - JOUR
AU  - Bezbradica, Dejan
AU  - Ćorović, Jasmina J.
AU  - Prodanović, Radivoje
AU  - Milosavić, Nenad
AU  - Knežević, Zorica
PY  - 2005
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/778
AB  - An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit® with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit® among methods applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme.
AB  - U ovom radu je ispitana mogućnost primene metode za kovalentno vezivanje lipaze iz Candida rugosa za komercijalni polimerni nosač Eupergit® kojom se dobijaju stabilni i aktivni imobilisani enzimi. Vezivanje se odvija preko ugljenohidratne komponente enzima, koja je prethodno modifikovana oksidacijom pomoću perjodata, a ne preko proteinske komponente, koja je važna za katalitičku aktivnost enzima. Hidrolitička aktivnost na ovaj način imobilisane lipaze upoređena je sa aktivnostima lipaza koje su imobilisane pomoću dve konvencionalne metode (vezivanje preko epoksidnih grupa nosača i vezivanje za nosač modifikovan glutaraldehidom). Rezultati ovog istraživanja pokazuju da je perjodatna metoda pogodnija za imobilizaciju lipaze na Eupergit® sa oba ispitivana aspekta: prinosa imobilizacije i hidrolitičke aktivnosti imobilisanog enzima.
PB  - Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Covalent immobilization of lipase from Candida rugosa on Eupergit®
T1  - Kovalentna imobilizacija lipaze iz Candida rugosa za Eupergit®
EP  - 186
IS  - 36
SP  - 179
DO  - 10.2298/APT0536179B
ER  - 

@article{
author = "Bezbradica, Dejan and Ćorović, Jasmina J. and Prodanović, Radivoje and Milosavić, Nenad and Knežević, Zorica",
year = "2005",
abstract = "An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit® with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit® among methods applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme., U ovom radu je ispitana mogućnost primene metode za kovalentno vezivanje lipaze iz Candida rugosa za komercijalni polimerni nosač Eupergit® kojom se dobijaju stabilni i aktivni imobilisani enzimi. Vezivanje se odvija preko ugljenohidratne komponente enzima, koja je prethodno modifikovana oksidacijom pomoću perjodata, a ne preko proteinske komponente, koja je važna za katalitičku aktivnost enzima. Hidrolitička aktivnost na ovaj način imobilisane lipaze upoređena je sa aktivnostima lipaza koje su imobilisane pomoću dve konvencionalne metode (vezivanje preko epoksidnih grupa nosača i vezivanje za nosač modifikovan glutaraldehidom). Rezultati ovog istraživanja pokazuju da je perjodatna metoda pogodnija za imobilizaciju lipaze na Eupergit® sa oba ispitivana aspekta: prinosa imobilizacije i hidrolitičke aktivnosti imobilisanog enzima.",
publisher = "Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Covalent immobilization of lipase from Candida rugosa on Eupergit®, Kovalentna imobilizacija lipaze iz Candida rugosa za Eupergit®",
pages = "186-179",
number = "36",
doi = "10.2298/APT0536179B"
}

Bezbradica, D., Ćorović, J. J., Prodanović, R., Milosavić, N.,& Knežević, Z.. (2005). Covalent immobilization of lipase from Candida rugosa on Eupergit®. in Acta periodica technologica
Faculty of Technology, Novi Sad.(36), 179-186.
https://doi.org/10.2298/APT0536179B

Bezbradica D, Ćorović JJ, Prodanović R, Milosavić N, Knežević Z. Covalent immobilization of lipase from Candida rugosa on Eupergit®. in Acta periodica technologica. 2005;(36):179-186.
doi:10.2298/APT0536179B .

Bezbradica, Dejan, Ćorović, Jasmina J., Prodanović, Radivoje, Milosavić, Nenad, Knežević, Zorica, "Covalent immobilization of lipase from Candida rugosa on Eupergit®" in Acta periodica technologica, no. 36 (2005):179-186,
https://doi.org/10.2298/APT0536179B . .