Stojanović, Željko

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a87e2854-298b-4b5e-978b-26ae361530a4
  • Stojanović, Željko (3)

Author's Bibliography

Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol

Pantić, Nevena; Spasojević, Milica; Stojanović, Željko; Veljović, Đorđe; Krstić, Jugoslav; Balaž, Ana Marija; Prodanović, Radivoje; Prodanović, Olivera

(Springer, 2022)

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
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 . .

Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics

Prokopijević, Miloš; Prodanović, Olivera; Spasojević, Dragica; Stojanović, Željko; Radotić, Ksenija; Prodanović, Radivoje

(Springer, New York, 2014)

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1768
AB  - Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics
VL  - 37
IS  - 5
SP  - 799
EP  - 804
DO  - 10.1007/s00449-013-1050-z
UR  - Kon_2651
ER  - 
@article{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Stojanović, Željko and Radotić, Ksenija and Prodanović, Radivoje",
year = "2014",
abstract = "Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics",
volume = "37",
number = "5",
pages = "799-804",
doi = "10.1007/s00449-013-1050-z",
url = "Kon_2651"
}
Prokopijević, M., Prodanović, O., Spasojević, D., Stojanović, Ž., Radotić, K.,& Prodanović, R.. (2014). Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. in Bioprocess and Biosystems Engineering
Springer, New York., 37(5), 799-804.
https://doi.org/10.1007/s00449-013-1050-z
Kon_2651
Prokopijević M, Prodanović O, Spasojević D, Stojanović Ž, Radotić K, Prodanović R. Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. in Bioprocess and Biosystems Engineering. 2014;37(5):799-804.
doi:10.1007/s00449-013-1050-z
Kon_2651 .
Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Stojanović, Željko, Radotić, Ksenija, Prodanović, Radivoje, "Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics" in Bioprocess and Biosystems Engineering, 37, no. 5 (2014):799-804,
https://doi.org/10.1007/s00449-013-1050-z .,
Kon_2651 .
17
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Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers

Prodanović, Olivera; Prokopijević, Miloš; Spasojević, Dragica; Stojanović, Željko; Radotić, Ksenija; Knezevic-Jugovic, Zorica D.; Prodanović, Radivoje

(Humana Press Inc, Totowa, 2012)

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Knezevic-Jugovic, Zorica D.
AU  - Prodanović, Radivoje
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1552
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  - Humana Press Inc, Totowa
T2  - Applied Biochemistry and Biotechnology
T1  - Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers
VL  - 168
IS  - 5
SP  - 1288
EP  - 1301
DO  - 10.1007/s12010-012-9857-7
UR  - Kon_2383
ER  - 
@article{
author = "Prodanović, Olivera and Prokopijević, Miloš and Spasojević, Dragica and Stojanović, Željko and Radotić, Ksenija and Knezevic-Jugovic, Zorica D. 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 = "Humana Press Inc, Totowa",
journal = "Applied Biochemistry and Biotechnology",
title = "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers",
volume = "168",
number = "5",
pages = "1288-1301",
doi = "10.1007/s12010-012-9857-7",
url = "Kon_2383"
}
Prodanović, O., Prokopijević, M., Spasojević, D., Stojanović, Ž., Radotić, K., Knezevic-Jugovic, Z. D.,& Prodanović, R.. (2012). Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology
Humana Press Inc, Totowa., 168(5), 1288-1301.
https://doi.org/10.1007/s12010-012-9857-7
Kon_2383
Prodanović O, Prokopijević M, Spasojević D, Stojanović Ž, Radotić K, Knezevic-Jugovic ZD, 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
Kon_2383 .
Prodanović, Olivera, Prokopijević, Miloš, Spasojević, Dragica, Stojanović, Željko, Radotić, Ksenija, Knezevic-Jugovic, Zorica D., 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 .,
Kon_2383 .
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