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標題: Characterization and heterologous expression of a novel lysophospholipase gene from Antrodia cinnamomea
作者: Hsu, K.H.
Wang, S.Y.
Chu, F.H.
Shaw, J.F.
關鍵字: Antrodia cinnamomea;esterase;expression;lysophospholipase;lysophosphatidic acid;pseudomonas-fluorescens;basidiomatal formation;camphorata mycelia;cdna cloning;proteins;lipase;polysaccharides;phospholipases;cells
Project: Journal of Applied Microbiology
期刊/報告no:: Journal of Applied Microbiology, Volume 108, Issue 5, Page(s) 1712-1722.
Aims: A novel lysophospholipase (LysoPL) from the basidiomycetous fungi Antrodia cinnamomea named ACLysoPL was cloned, heteroexpressed in Escherichia coli and characterized. Methods and Results: The gene encoding ACLysoPL was obtained from expressed sequence tags from A. cinnamomea. The full length of this gene has a 945 -bp open reading frame encoding 314 amino acids with a molecular weight of 35 center dot 5 kDa. ACLysoPL contains a lipase consensus sequence (GXSXG) motif and a Ser-His-Asp catalytic triad. A putative peroxisomal targeting signal type 1 was found in the C-terminal. Heterologous expression of ACLysoPL in E. coli showed that the enzyme preferentially hydrolyses long-chain acyl esterases at pH 7 and 30 degrees C. ACLysoPL is a psychrophilic enzyme about 40% of whose maximum activity remained at 4 degrees C. The LysoPL activities with lysophospholipids as substrate were analysed by gas chromatography/mass spectrometry. Conclusion: We have identified and characterized a gene named ACLysoPL encoding a protein performing LysoPL and esterase activities. Significance and Impact of the Study: This is the first LysoPL of A. cinnamomea identified and characterized at the molecular level.
ISSN: 1364-5072
DOI: 10.1111/j.1365-2672.2009.04569.x
Appears in Collections:食品暨應用生物科技學系

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