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Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal

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2022
Proceedings_EcoTER22_376-381.pdf (19.17Mb)
Authors
Pantić, Nevena
Spasojević, Milica
Prokopijević, Miloš
Spasojević, Dragica
Balaž, Ana Marija
Prodanović, Radivoje
Prodanović, Olivera
Conference object (Published version)
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Abstract
For the purpose of immobilization, one of the most commonly used enzymes is horseradish peroxidase (HRP). Different carriers can be used as supports for the immobilization of HRP: alginate, pectin, magnetic-beads, macroporous copolymers, silicas etc. Covalent binding of an enzyme to the carrier leads to the formation of strong linkage, thus preventing the enzyme leakage. Macroporous copolymers with different porous characteristics were used for the immobilization of horseradish peroxidase by employing periodate and glutaraldehyde method. Five and 25 mg of HRP were immobilized per gram of the copolymer. Increasing the amount of added enzyme leads to the increase of specific activity of immobilized enzyme. Copolymer with the pore diameter of 297 nm showed the most promising results in terms of specific activity. Immobilized enzymes can be used for the removal of phenolic compounds from waste effluents.
Keywords:
macroporous copolymer / periodate immobilization / horseradish peroxidase / dispersion polymerization / phenol removal
Source:
29th International Conference Ecological Truth and Environmental Research, 2022, 354-359
Publisher:
  • University of Belgrade, Technical Faculty in Bor
Funding / projects:
  • Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 200053 (University of Belgrade, Institute for Multidisciplinary Research) (RS-200053)

ISBN: 978-86-6305-123-2

[ Google Scholar ]
Handle
https://hdl.handle.net/21.15107/rcub_rimsi_1774
URI
http://rimsi.imsi.bg.ac.rs/handle/123456789/1774
Collections
  • Radovi istraživača / Researchers’ publications
Institution/Community
Institut za multidisciplinarna istraživanja
TY  - CONF
AU  - Pantić, Nevena
AU  - Spasojević, Milica
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1774
AB  - For the purpose of immobilization, one of the most commonly used enzymes is horseradish peroxidase (HRP). Different carriers can be used as supports for the immobilization of HRP: alginate, pectin, magnetic-beads, macroporous copolymers, silicas etc. Covalent binding of an enzyme to the carrier leads to the formation of strong linkage, thus preventing the enzyme leakage. Macroporous copolymers with different porous characteristics were used for the immobilization of horseradish peroxidase by employing periodate and glutaraldehyde method. Five and 25 mg of HRP were immobilized per gram of the copolymer. Increasing the amount of added enzyme leads to the increase of specific activity of immobilized enzyme. Copolymer with the pore diameter of 297 nm showed the most promising results in terms of specific activity. Immobilized enzymes can be used for the removal of phenolic compounds from waste effluents.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 29th International Conference Ecological Truth and Environmental Research
T1  - Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal
EP  - 359
SP  - 354
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_1774
ER  - 
@conference{
author = "Pantić, Nevena and Spasojević, Milica and Prokopijević, Miloš and Spasojević, Dragica and Balaž, Ana Marija and Prodanović, Radivoje and Prodanović, Olivera",
year = "2022",
abstract = "For the purpose of immobilization, one of the most commonly used enzymes is horseradish peroxidase (HRP). Different carriers can be used as supports for the immobilization of HRP: alginate, pectin, magnetic-beads, macroporous copolymers, silicas etc. Covalent binding of an enzyme to the carrier leads to the formation of strong linkage, thus preventing the enzyme leakage. Macroporous copolymers with different porous characteristics were used for the immobilization of horseradish peroxidase by employing periodate and glutaraldehyde method. Five and 25 mg of HRP were immobilized per gram of the copolymer. Increasing the amount of added enzyme leads to the increase of specific activity of immobilized enzyme. Copolymer with the pore diameter of 297 nm showed the most promising results in terms of specific activity. Immobilized enzymes can be used for the removal of phenolic compounds from waste effluents.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "29th International Conference Ecological Truth and Environmental Research",
title = "Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal",
pages = "359-354",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_1774"
}
Pantić, N., Spasojević, M., Prokopijević, M., Spasojević, D., Balaž, A. M., Prodanović, R.,& Prodanović, O.. (2022). Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal. in 29th International Conference Ecological Truth and Environmental Research
University of Belgrade, Technical Faculty in Bor., 354-359.
https://hdl.handle.net/21.15107/rcub_rimsi_1774
Pantić N, Spasojević M, Prokopijević M, Spasojević D, Balaž AM, Prodanović R, Prodanović O. Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal. in 29th International Conference Ecological Truth and Environmental Research. 2022;:354-359.
https://hdl.handle.net/21.15107/rcub_rimsi_1774 .
Pantić, Nevena, Spasojević, Milica, Prokopijević, Miloš, Spasojević, Dragica, Balaž, Ana Marija, Prodanović, Radivoje, Prodanović, Olivera, "Covalent immobilization of horseradish peroxidase on novel macroporous poly(GMA-co-EGDMA) for phenol removal" in 29th International Conference Ecological Truth and Environmental Research (2022):354-359,
https://hdl.handle.net/21.15107/rcub_rimsi_1774 .

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