Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization

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Title
Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization
Author(s)
S P Hwang; Jungoh Ahn; S M Lee; T G Lee; S J Haam; K T Lee; I S Ahn; Joon Ki Jung
Bibliographic Citation
Biotechnology Letters, vol. 26, no. 7, pp. 603-605
Publication Year
2004
Abstract
A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.
Keyword
AdsorptionAvicelCellulose-binding domainImmobilizationLipase
ISSN
0141-5492
Publisher
Springer
DOI
http://dx.doi.org/10.1023/B:BILE.0000021964.69500.6f
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
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