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.
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
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