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Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin

Extracellular keratinase isolated from Aspergillus flavus K-03 was immobilized on calcium alginate. The properties and reaction activities of free and immobilized keratinase with calcium alginate were characterized. The immobilized keratinase showed proteolytic activity against soluble azo-casein an...

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Autor principal: Kim, Jeong-Dong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Society of Mycology 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774865/
https://www.ncbi.nlm.nih.gov/pubmed/24049486
http://dx.doi.org/10.4489/MYCO.2005.33.2.121
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author Kim, Jeong-Dong
author_facet Kim, Jeong-Dong
author_sort Kim, Jeong-Dong
collection PubMed
description Extracellular keratinase isolated from Aspergillus flavus K-03 was immobilized on calcium alginate. The properties and reaction activities of free and immobilized keratinase with calcium alginate were characterized. The immobilized keratinase showed proteolytic activity against soluble azo-casein and azo-keratin, and insoluble feather keratin. Heat stability and pH tolerance of keratinase were greatly enhanced by immobilization. It also displayed a higher level of heat stability and an increased tolerance toward alkaline pHs compared with free keratinase. During the durability test at 40℃, 48% of the original enzyme activity of the immobilized keratinase was remained after 7 days of incubation. The immobilized keratinase exhibited better stability, thus increasing its potential for use in industrial application.
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spelling pubmed-37748652013-09-18 Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin Kim, Jeong-Dong Mycobiology Note Extracellular keratinase isolated from Aspergillus flavus K-03 was immobilized on calcium alginate. The properties and reaction activities of free and immobilized keratinase with calcium alginate were characterized. The immobilized keratinase showed proteolytic activity against soluble azo-casein and azo-keratin, and insoluble feather keratin. Heat stability and pH tolerance of keratinase were greatly enhanced by immobilization. It also displayed a higher level of heat stability and an increased tolerance toward alkaline pHs compared with free keratinase. During the durability test at 40℃, 48% of the original enzyme activity of the immobilized keratinase was remained after 7 days of incubation. The immobilized keratinase exhibited better stability, thus increasing its potential for use in industrial application. The Korean Society of Mycology 2005-06 2005-06-30 /pmc/articles/PMC3774865/ /pubmed/24049486 http://dx.doi.org/10.4489/MYCO.2005.33.2.121 Text en Copyright © 2005 by The Korean Society of Mycology http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Note
Kim, Jeong-Dong
Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
title Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
title_full Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
title_fullStr Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
title_full_unstemmed Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
title_short Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
title_sort immobilization of keratinase from aspergillus flavus k-03 for degradation of feather keratin
topic Note
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774865/
https://www.ncbi.nlm.nih.gov/pubmed/24049486
http://dx.doi.org/10.4489/MYCO.2005.33.2.121
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