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Updated: Jun 19, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Characterization and heterologous expression of a novel lysophospholipase gene from Antrodia cinnamomea
1School of Forestry and Resource Conservation, Nation Taiwan University, Taipei, Taiwan.
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 35.5 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.
