Biochemical properties and substrate specificity of lipase from Staphylococcus aureus B56

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Title
Biochemical properties and substrate specificity of lipase from Staphylococcus aureus B56
Author(s)
Woo Hyuk Jung; Hyung Kwoun Kim; Chan Yong Lee; Tae Kwang Oh
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 12, no. 1, pp. 25-30
Publication Year
2002
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°C and pH 8-8.5, respectively. The enzyme was stable up to 55°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.
Keyword
lipasestaphylococcus aureussubstrate specificity
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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