Collagen-Immobilized Lipases Show Good Activity and Reusability for Butyl Butyrate Synthesis.

Abstract

Candida rugosa lipases were immobilized onto collagen fibers through glutaraldehyde cross-linking method. The immobilization process has been optimized. Under the optimal immobilization conditions, the activity of the collagen-immobilized lipase reached 340U/g. The activity was recovered of 28.3% by immobilization. The operational stability of the obtained collagen-immobilized lipase for hydrolysis of olive oil emulsion was determined. The collagen-immobilized lipase showed good tolerance to temperature and pH variations in comparison to free lipase. The collagen-immobilized lipase was also applied as biocatalyst for synthesis of butyl butyrate from butyric acid and 1-butanol in n-hexane. The conversion yield was 94% at the optimal conditions. Of its initial activity, 64% was retained after 5cycles for synthesizing butyl butyrate in n-hexane.