Overexpression of thermoalkalophilic lipase from Bacillus stearothermophilus L1 in Saccharomyces cerevisiae

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Title
Overexpression of thermoalkalophilic lipase from Bacillus stearothermophilus L1 in Saccharomyces cerevisiae
Author(s)
Jung Oh Ahn; H W Jang; Hong-Weon Lee; Eui Sung Choi; S J Haam; Tae Kwang Oh; Joon Ki Jung
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 13, no. 3, pp. 451-456
Publication Year
2003
Abstract
An expression vector system was developed for the secretory production of recombinant Bacillus stearothermophilus L1 lipase in Saccharomyces cerevisiae. The mature L1 lipase gene was fused to α-amylase signal sequence from Aspergillus oryzae for the effective secretion into the culture broth and the expression was controlled under GAL10 (the gene coding UDP-galactose epimerase of S. cerevisiae) promoter. S. cerevisiae harboring the resulting plasmid successfully secreted L1 lipase into the culture broth. To examine an optimum condition for L1 lipase expression in the fed-batch culture, L1 lipase expression was induced at three different growth phases (early, mid, and late-exponential growth phases). Maximum production of L1 lipase (1,254,000 U/l, corresponding to 0.65/l) was found when the culture was induced at an early growth phase. Secreted recombinant L1 lipase was purified only through CM-Sepharose chromatography, and the purified enzyme showed 1,963 U/mg of specific activity and thermoalkalophilic properties similar to those reported for the enzyme expressed in Escherichia coli.
Keyword
bacillus stearothermophilus L1induction timesaccharomyces cerevisiaethermoalkalophilic lipase
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
Division of Bio Technology Innovation > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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