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 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.
Department of Life Science, Hanyang University, Seoul 133-791, Korea.
Jeong-Dong
JD
Kim
Durability; Heat stability; Immobilization; Keratinase; pH tolerance