Your browser doesn't support javascript.
loading
Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin
Mycobiology ; : 121-123, 2005.
Article in English | WPRIM | ID: wpr-730058
ABSTRACT
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 40degrees C, 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.
Subject(s)

Full text: Available Index: WPRIM (Western Pacific) Main subject: Aspergillus / Aspergillus flavus / Calcium / Feathers / Hot Temperature / Hydrogen-Ion Concentration / Immobilization Limits: Animals Language: English Journal: Mycobiology Year: 2005 Type: Article

Similar

MEDLINE

...
LILACS

LIS

Full text: Available Index: WPRIM (Western Pacific) Main subject: Aspergillus / Aspergillus flavus / Calcium / Feathers / Hot Temperature / Hydrogen-Ion Concentration / Immobilization Limits: Animals Language: English Journal: Mycobiology Year: 2005 Type: Article