Characterization of an alkaline lipase from Proteus vulgaris K80 and the DNA sequence of the encoding gene

Cited 0 time in scopus
Metadata Downloads
Title
Characterization of an alkaline lipase from Proteus vulgaris K80 and the DNA sequence of the encoding gene
Author(s)
Hyung Kwoun Kim; Jung Kee Lee; Hyoung Man Kim; Tae Kwang Oh
Bibliographic Citation
FEMS Microbiology Letters, vol. 135, pp. 117-121
Publication Year
1996
Abstract
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 hydrolytic 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.
Keyword
alkaline enzymeenterobacteriumlipase genelipase K80proteus vulgaris
ISSN
0378-1097
Publisher
Oxford Univ Press
DOI
http://dx.doi.org/10.1111/j.1574-6968.1996.tb07975.x
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.