Publication: Molecular cloning and functional expression of a novel extracellular lipase from the thermotolerant yeast Candida thermophila
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Issued Date
2007-03-01
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ISSN
15671364
15671356
15671356
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2-s2.0-33846953553
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Mahidol University
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SCOPUS
Bibliographic Citation
FEMS Yeast Research. Vol.7, No.2 (2007), 232-243
Suggested Citation
Jantaporn Thongekkaew, Chuenchit Boonchird Molecular cloning and functional expression of a novel extracellular lipase from the thermotolerant yeast Candida thermophila. FEMS Yeast Research. Vol.7, No.2 (2007), 232-243. doi:10.1111/j.1567-1364.2006.00173.x Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/24569
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Title
Molecular cloning and functional expression of a novel extracellular lipase from the thermotolerant yeast Candida thermophila
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Abstract
The thermotolerant yeast Candida thermophila SRY-09 isolated from Thailand produces an extracellular lipase that hydrolyses various triglycerides. To clone the gene encoding the lipase, Saccharomyces cerevisiae was transformed with a C. thermophila genomic library and screened for lipase activity on medium containing olive oil emulsion and rhodamine B. One C. thermophila lipase gene (CtLIP) was found that contained an ORF of 1317 bp encoding a deduced polypeptide of 438 amino acids. Candida thermophila lipase contained a Gly-Asp-Ser-Gln-Gly motif which matched the consensus Gly-X-Ser-X-Gly conserved among lipolytic enzymes. Heterologous expression of the cloned CtLIP under the control of the alcohol oxidase gene (AOX1) promoter in the methylotrophic yeast Pichia pastoris, and enzymatic measurements confirmed the function of the respective protein as a lipase. The recombinant CtLIP could hydrolyse various substrates at high temperature (55°C) with higher efficiency than at 37 or 45°C and preferentially hydrolysed two-positional ester bonds. As with C. thermophila, the heterologously expressed lipase was secreted into the medium by Pichia pastoris. © 2006 Federation of European Microbiological Societies.