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 . .