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KMID : 0545120000100050656
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Journal of Microbiology and Biotechnology
2000 Volume.10 No. 5 p.656 ~ p.662
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Staphylococcus haemolyticus Lipase
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Oh, Byung Chul
Kim, Hyung Kwoun/Kim, Myung Hee/Lee, Jung Kee/Oh, Tae Kwang
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Abstract
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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 70,800U/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 (∼180kDa) 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.
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