Mycobiology.  2005 Jun;33(2):121-123.

Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin

Affiliations
  • 1Department of Life Science, Hanyang University, Seoul 133-791, Korea. jdkim@hanyang.ac.kr

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.

Keyword

Durability; Heat stability; Immobilization; Keratinase; pH tolerance

MeSH Terms

Animals
Aspergillus flavus*
Aspergillus*
Calcium
Feathers*
Hot Temperature
Hydrogen-Ion Concentration
Immobilization*
Calcium
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