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

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

Content Provider	Semantic Scholar
Author	Hwang, Sangpill Ahn, Jungoh Lee, Sumin Haam, Seungjoo Lee, Kwang Y. Ahn, Ik-Sung Jung, Joon-Ki
Copyright 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.
Starting Page	603
Ending Page	605
Page Count	3
File Format	PDF HTM / HTML
DOI	10.1023/B:BILE.0000021964.69500.6f
PubMed reference number	15168862
Journal	Medline
Volume Number	26
Alternate Webpage(s)	http://web.yonsei.ac.kr/hg/Biotechnology%20Letters-2004.pdf
Alternate Webpage(s)	https://page-one.springer.com/pdf/preview/10.1023/B:BILE.0000021964.69500.6f
Alternate Webpage(s)	https://doi.org/10.1023/B%3ABILE.0000021964.69500.6f
Journal	Biotechnology Letters
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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