Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin.
- Author:
Jeong Dong KIM
1
Author Information
1. Department of Life Science, Hanyang University, Seoul 133-791, Korea. jdkim@hanyang.ac.kr
- Publication Type:Brief Communication
- Keywords:
Durability;
Heat stability;
Immobilization;
Keratinase;
pH tolerance
- MeSH:
Animals;
Aspergillus flavus*;
Aspergillus*;
Calcium;
Feathers*;
Hot Temperature;
Hydrogen-Ion Concentration;
Immobilization*
- From:Mycobiology
2005;33(2):121-123
- CountryRepublic of Korea
- Language:English
-
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.
