Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier
A series of poly(GMA-co-EGDMA) resins with identical composition but varying particle sizes, pore radii, specific surface areas and specific volumes are studied to assess how Candida antarctica lipase B immobilization affects the porosity of the copolymer particles. Mercury porosimetry reveals a sig...
Published in: | Macromolecular Bioscience |
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Main Authors: | , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2011
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Subjects: | |
Online Access: | https://scidar.kg.ac.rs/handle/123456789/19850 https://doi.org/10.1002/mabi.201100127 |
_version_ | 1821691038037704704 |
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author | Miletic, Nemanja Vuković, Zorica Nastasović, Aleksandra Loos, Katja |
author_facet | Miletic, Nemanja Vuković, Zorica Nastasović, Aleksandra Loos, Katja |
author_sort | Miletic, Nemanja |
collection | SCIDAR - A Digital Archive of the University of Kragujevac |
container_issue | 11 |
container_start_page | 1537 |
container_title | Macromolecular Bioscience |
container_volume | 11 |
description | A series of poly(GMA-co-EGDMA) resins with identical composition but varying particle sizes, pore radii, specific surface areas and specific volumes are studied to assess how Candida antarctica lipase B immobilization affects the porosity of the copolymer particles. Mercury porosimetry reveals a significant change in the average pore size (up to 6.1-fold), the specific surface area (up to 3.2-fold) and the specific volume (up to 2.1-fold) of the epoxy resin. A similar behaviour is observed for glutaraldehyde-modified epoxy resins. The influences of the resin porosity properties on the loading of Candida antarctica lipase B during immobilization and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized lipase are studied. Published |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
id | ftunivkragujevac:oai:https://scidar.kg.ac.rs:123456789/19850 |
institution | Open Polar |
language | English |
op_collection_id | ftunivkragujevac |
op_container_end_page | 1543 |
op_doi | https://doi.org/10.1002/mabi.201100127 |
op_relation | Macromolecular bioscience Miletić, N., Vuković, Z., Nastasović, A., Loos, K. (2011): Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier. Macromolecular Bioscience, 11(11), 1537-1543. 1616-5187 https://scidar.kg.ac.rs/handle/123456789/19850 doi:10.1002/mabi.201100127 000297555500011 |
publishDate | 2011 |
publisher | Wiley |
record_format | openpolar |
spelling | ftunivkragujevac:oai:https://scidar.kg.ac.rs:123456789/19850 2025-01-16T19:15:05+00:00 Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier Miletic, Nemanja Vuković, Zorica Nastasović, Aleksandra Loos, Katja 2011 application/pdf https://scidar.kg.ac.rs/handle/123456789/19850 https://doi.org/10.1002/mabi.201100127 en eng Wiley Macromolecular bioscience Miletić, N., Vuković, Z., Nastasović, A., Loos, K. (2011): Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier. Macromolecular Bioscience, 11(11), 1537-1543. 1616-5187 https://scidar.kg.ac.rs/handle/123456789/19850 doi:10.1002/mabi.201100127 000297555500011 Candida antarctica Lipase B Immobilization Epoxy carrier Glutaraldehyde modification Porosity poly[(glycidyl methacrylate)-co-(ethylene glycol dimethacrylate)] article PublishedVersion 2011 ftunivkragujevac https://doi.org/10.1002/mabi.201100127 2024-01-16T17:23:29Z A series of poly(GMA-co-EGDMA) resins with identical composition but varying particle sizes, pore radii, specific surface areas and specific volumes are studied to assess how Candida antarctica lipase B immobilization affects the porosity of the copolymer particles. Mercury porosimetry reveals a significant change in the average pore size (up to 6.1-fold), the specific surface area (up to 3.2-fold) and the specific volume (up to 2.1-fold) of the epoxy resin. A similar behaviour is observed for glutaraldehyde-modified epoxy resins. The influences of the resin porosity properties on the loading of Candida antarctica lipase B during immobilization and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized lipase are studied. Published Article in Journal/Newspaper Antarc* Antarctica SCIDAR - A Digital Archive of the University of Kragujevac Macromolecular Bioscience 11 11 1537 1543 |
spellingShingle | Candida antarctica Lipase B Immobilization Epoxy carrier Glutaraldehyde modification Porosity poly[(glycidyl methacrylate)-co-(ethylene glycol dimethacrylate)] Miletic, Nemanja Vuković, Zorica Nastasović, Aleksandra Loos, Katja Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier |
title | Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier |
title_full | Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier |
title_fullStr | Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier |
title_full_unstemmed | Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier |
title_short | Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier |
title_sort | effect of candida antarctica lipase b immobilization on the porous structure of the carrier |
topic | Candida antarctica Lipase B Immobilization Epoxy carrier Glutaraldehyde modification Porosity poly[(glycidyl methacrylate)-co-(ethylene glycol dimethacrylate)] |
topic_facet | Candida antarctica Lipase B Immobilization Epoxy carrier Glutaraldehyde modification Porosity poly[(glycidyl methacrylate)-co-(ethylene glycol dimethacrylate)] |
url | https://scidar.kg.ac.rs/handle/123456789/19850 https://doi.org/10.1002/mabi.201100127 |