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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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Detalles Bibliográficos
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
Descripción
Sumario: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.