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Title 

Biochemical properties and substrate specificity of lipase from Staphylococcus aureus B56

Authors 

Woo Hyuk JungHyung Kwoun KimChan Yong LeeTae Kwang Oh

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2002

Citation 

Journal of Microbiology and Biotechnology, vol. 12, no. 1, pp. 25-30

Keywords 

lipasestaphylococcus aureussubstrate specificitytriacylglycerol lipaseenzyme specificitystaphylococcus haemolyticusstaphylococcus

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.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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