Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Staphylococcus haemolyticus Lipase; High-Level Expression in Escherichia coli and Activation of Nonionic Detergent

  • Oh, Byung-Chul (Environmental Bioresources Lab., Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Hyung-Kwoun (Environmental Bioresources Lab., Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Myung-Hee (Environmental Bioresources Lab., Korea Research Institute of Bioscience and Biotechnology) ;
  • Lee, Jung-Kee (Environmental Bioresources Lab., Korea Research Institute of Bioscience and Biotechnology) ;
  • Oh, Tae-Kwang (Environmental Bioresources Lab., Korea Research Institute of Bioscience and Biotechnology)
  • Published : 2000.10.01
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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 protein. 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 the towards the medium and the long-chain saturated triglycerides.

Keywords

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