Staphylococcus haemolyticus lipase: high-level expression in Escherichia coli and activation of nonionic detergent

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Title
Staphylococcus haemolyticus lipase: high-level expression in Escherichia coli and activation of nonionic detergent
Author(s)
Byung Chul Oh; Hyung Kwoun Kim; Myung Hee Kim; Jung Kee Lee; Tae Kwang Oh
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 10, no. 5, pp. 656-662
Publication Year
2000
Abstract
A high level of Staphylococcus haemolyticus L62 lipase was expressed in an Escherichia coli transformant. The expressed lipase activity in the cell-free extract was 70,800 U/l, which corresponded to 30% of the total cellular proteins. Pre-mixing of the L62 lipase with some nonionic detergents enhanced its hydrolytic activity towards olive oil: Tween detergents activated the L62 lipase by 3 fold. Gel filtration chromatography of the Tween-80-L62 lipase mixture demonstrated a polymerized complex (~180 kDa) formed exclusively between Tween-80 and the L62 lipase. The lipase enzyme in the complex showed a higher specific activity towards most triacylglycerols than the intact L62 lipase. The activity enhancement towards each substrate was quite different depending on the acyl chain length; the activity towards tributyrin, trilinolein, and trilinolenin was much more enhanced than that towards the medium and the long-chain saturated triglycerides.
Keyword
LipaseStaphylococcus haemolyticusnonionic detergent
ISSN
1017-7825
Publisher
South Korea
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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