Kim_2015_J.Microbiol.Biotechnol_25_2024

Reference

Title : Characterization of an Alkaline Family I.4 Lipase from Bacillus sp. W130-35 Isolated from a Tidal Mud Flat with Broad Substrate Specificity - Kim_2015_J.Microbiol.Biotechnol_25_2024
Author(s) : Kim HJ , Jung WK , Lee HW , Yoo W , Kim TD , Kim H
Ref : J Microbiol Biotechnol , 25 :2024 , 2015
Abstract :

A gene encoding lipolytic enzyme, lip7-3, was isolated from Bacillus sp. W130-35 isolated from a tidal mud flat. The gene encoded a protein of 215 amino acids with a signal peptide composed of 34 amino acid residues. Lip7-3 belonged to the family I.4 lipase and showed its maximal activity at pH 9.0 and 60 degrees C. Its activity increased in the presence of 30% methanol and, remarkably, increased as well to 154.6% in the presence of Ca(2+). Lip7-3 preferred pnitrophenyl octanoate (C8) as a substrate and exhibited broad specificity for short- to longchain fatty acid esters. Additionally, Lip7-3 showed a low degree of enantioselectivity for an S-enantiomer (e.g., (S)-methyl-3-hydroxy-2-methylpropionate). It efficiently hydrolyzed glyceryl tributyrate, but did not hydrolyze glyceryl trioleate, fish oil, or olive oil. Its substrate specificity and activation by the solvent might offer a merit to the biotechnological enzyme applications like transesterification in the production of biodiesel.

PubMedSearch : Kim_2015_J.Microbiol.Biotechnol_25_2024
PubMedID: 26370800
Gene_locus related to this paper: bacpu-w8rkh7

Citations formats

Kim HJ, Jung WK, Lee HW, Yoo W, Kim TD, Kim H (2015)
Characterization of an Alkaline Family I.4 Lipase from Bacillus sp. W130-35 Isolated from a Tidal Mud Flat with Broad Substrate Specificity
J Microbiol Biotechnol 25 :2024

Kim HJ, Jung WK, Lee HW, Yoo W, Kim TD, Kim H (2015)
J Microbiol Biotechnol 25 :2024