Characterization and heterologous expression of a novel lysophospholipase gene from Antrodia cinnamomea.
J Appl Microbiol
; 108(5): 1712-22, 2010 May.
Article
in En
| MEDLINE
| ID: mdl-19849771
ABSTRACT
AIMS:
A novel lysophospholipase (LysoPL) from the basidiomycetous fungi Antrodia cinnamomea named ACLysoPL was cloned, heteroexpressed in Escherichia coli and characterized. METHODS ANDRESULTS:
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Antrodia
/
Lysophospholipase
Language:
En
Journal:
J Appl Microbiol
Journal subject:
MICROBIOLOGIA
Year:
2010
Document type:
Article
Affiliation country:
Taiwan