Open AccessCharacterization of an alkaline lipase from Proteus vulgaris K80 and the DNA sequence of the encoding gene
Author(s) -
Kim HyungKwoun,
Lee JungKee,
Kim Hyoungman,
Oh TaeKwang
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb07975.x
Subject(s) - lipase , proteus vulgaris , open reading frame , biochemistry , gene , pseudomonas , peptide sequence , molecular cloning , biology , escherichia coli , sequence analysis , molecular mass , chemistry , microbiology and biotechnology , enzyme , bacteria , genetics
A facultatively anaerobic bacterium producing an extracellular alkaline lipase was isolated from the soil collected near a sewage disposal plant in Korea and identified to be a strain of Proteus vulgaris . The molecular mass of the purified lipase K80 was estimated to be 31 kDa by SDS‐PAGE. It was found to be an alkaline enzyme having maximum hydrolytid activity at pH 10, while fairly stable in a wide pH range from 5 to 11. The gene for lipase K80 was cloned in Escherichia coli . Sequence analysis showed an open reading frame of 861 bp coding for a polypeptide of 287 amino acid residues. The deduced amino acid sequence of the lipase gene had 46.3% identity to the lipase from Pseudomonas fragi .