Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Biochemical Properties and Substrate Specificity of Lipase from Staphylococcus aureus B56

  • Jung, Woo-Hyuk (Environmental Bioresources Laboratory, Korea Research Institute of Bioscience and Biotechnology, Department of Microbiology, Daejeon University) ;
  • Kim, Hyung-Kwoun (Environmental Bioresources Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
  • Lee, Chan-Yong (Department of Microbiology, Daejeon University) ;
  • Oh, Tae-Kwang (Environmental Bioresources Laboratory, Korea Research Institute of Bioscience and Biotechnology, Department of Microbiology, Daejeon University)
  • Published : 2002.02.01
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Abstract

A lipase of Staphylococcus aureus B56 was purified from a culture supernatant and its molecular weight was estimated to be 45 kDa by SDS-PAGE. The optimum temperature and pH for the hydrolysis of olive oil was $42^{\circ}C$ and pH 8-8.5, respectively. The enzyme was stable up to $55^{\circ}C$ in the presence of $Ca^++$ at pHs 5-11. The lipase gene was cloned using the PCR amplification method. The sequence analysis showed an open reading frame of 2,076 bp, which encoded a preproenzyme of 691 amino acids. The preproenzyme was composed of a signal sequence (37 aa), propeptide (255 aa), and mature enzyme (399 aa). Based on a sequence comparison, lipase B56 constituted of a separate subgroup among the staphylococcal lipase groups, such as S. aureus PS54 and S. haemolyticus L62 lipases, and was distinct from other lipases in their optimum pH and substrate specificity.

Keywords

References

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