RRC ID 47541
Author Cai J, Xie Y, Song B, Wang Y, Zhang Z, Feng Y.
Title Fervidobacterium changbaicum Lip1: identification, cloning, and characterization of the thermophilic lipase as a new member of bacterial lipase family V.
Journal Appl Microbiol Biotechnol
Abstract A novel lipase gene encoded 315 amino acid residues was obtained using lipase-prospecting primers and genome walking from hyperthermophilic bacterium Fervidobacterium changbaicum CBS-1. Sequence alignment and phylogenetic analysis revealed this novel lipase is a new member of bacterial lipase family V. The recombinant enzyme F. changbaicum lipase 1 (FCLip1) showed maximum activity at 78 °C and pH 7.8. It displayed extreme thermostability at 70 °C and was also stable across a wide pH range from 6.0 to 12.0. Kinetic study demonstrated FCLip1 preferentially hydrolyzed middle-length acyl chains, especially p-nitrophenyl caprate and tricaprylin. With p-nitrophenyl caprate as a substrate, the enzyme exhibited a K(m) and k(cat) of 4.67 μM and 22.7/s, respectively. In addition, FCLip1 was resistant to various detergents and organic solvents. This enzyme is the first reported thermophilic lipase from bacterial family Thermotogaceae. Its extreme stability with respect to temperature and pH, along with its triglyceride hydrolysis activity, indicate that FCLip1 has high potential for future application.
Volume 89(5)
Pages 1463-73
Published 2011-3-1
DOI 10.1007/s00253-010-2971-y
PMID 21046373
MeSH Amino Acid Sequence Bacteria / enzymology* Bacteria / genetics Cloning, Molecular Enzyme Stability Hot Temperature Hydrogen-Ion Concentration Kinetics Lipase / chemistry Lipase / genetics* Lipase / metabolism* Molecular Sequence Data Phylogeny Recombinant Proteins / chemistry Recombinant Proteins / genetics Recombinant Proteins / isolation & purification Recombinant Proteins / metabolism Sequence Analysis, DNA Sequence Homology, Amino Acid Substrate Specificity
IF 3.53
Times Cited 11
WOS Category BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Resource
General Microbes JCM 13353