Co-expression of an organic solvent-tolerant lipase and its cognate foldase of Pseudomonas aeruginosa CS-2 and the application of the immobilized recombinant lipase

Peng, R; Lin, J; Wei, D

HERO ID

1455163

Reference Type

Journal Article

Year

2011

Language

English

PMID

21720839

HERO ID 1455163
In Press No
Year 2011
Title Co-expression of an organic solvent-tolerant lipase and its cognate foldase of Pseudomonas aeruginosa CS-2 and the application of the immobilized recombinant lipase
Authors Peng, R; Lin, J; Wei, D
Journal Applied Biochemistry and Biotechnology
Volume 165
Issue 3-4
Page Numbers 926-937
Abstract The genes of CS-2 lipase and its cognate foldase were cloned from Pseudomonas aeruginosa CS-2. A stop codon was not found in the lipase gene. The amino acid sequence deduced from the lipase gene from P. aeruginosa CS-2 showed 97.8%, 71.3%, and 71.2% identity with lipases from P. aeruginosa LST-03, P seudomonas mendocina ymp, and Pseudomonas stutzeri A1501, respectively. The co-expression of CS-2 lipase and its cognate foldase of P. aeruginosa CS-2 in E scherichia coli BL21 (DE3) resulted in the formation of a soluble lipase. The recombinant lipase and foldase were purified to homogeneity using nickel affinity chromatography and about 10.2-fold with 40.9% recovery was achieved for the purification of the recombinant lipase. The molecular masses of the lipase and the foldase were estimated to be 35.7 and 38.3 kDa in SDS-PAGE, respectively. The recombinant lipase showed stability in the presence of some organic solvents. The recombinant CS-2 lipase was immobilized and subsequently used for the synthesis of butyl acetate in heptane. The conversion of substrate decreased from 98.2% to 87.4% after 5 cycles in reuse of the immobilized lipase.
Doi 10.1007/s12010-011-9309-9
Pmid 21720839
Wosid WOS:000296640000016
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:000296640000016
Is Public Yes
Language Text English
Keyword Lipase; Foldase; Pseudomonas aeruginosa; Butyl acetate