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Immobilization of Candida antarctica lipase B on the surface of modified sol-gel matrix

Authors
Yagonia, Camila Flor J.Park, KyungmoonYoo, Young Je
Issue Date
Mar-2014
Publisher
SPRINGER
Keywords
Sol-gel matrix; Covalent immobilization; Candida antarctica lipase B; Enzyme stability
Citation
JOURNAL OF SOL-GEL SCIENCE AND TECHNOLOGY, v.69, no.3, pp.564 - 570
Journal Title
JOURNAL OF SOL-GEL SCIENCE AND TECHNOLOGY
Volume
69
Number
3
Start Page
564
End Page
570
URI
https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/16735
DOI
10.1007/s10971-013-3257-5
ISSN
0928-0707
Abstract
The use of modified sol-gel matrix to immobilize the enzyme Candida antartica lipase B (CALB) was investigated. Free hydroxyl groups on the matrix surface were exploited to covalently immobilize the enzyme. Based from the results, incorporating hydrophobic sol-gel precursor (ethyltrimethoxysilane) enhanced enzyme activity. An enzyme activity of 192.02 U/g beads with 80.88 % attachment was obtained. At alkaline pH, immobilization yield of enzyme increased. The attachment of enzyme on the surface of the matrix was confirmed by scanning electron microscope images. Covalently immobilized CALB on sol-gel supports has higher thermal stability with 2.7 times higher half-life compared to soluble enzymes at 60 A degrees C. This enzyme immobilization system retains the enzyme residual activity even for repetitive use. Hence, the immobilization approach developed recommends its further application.
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