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http://dx.doi.org/10.4014/jmb.1507.07104

Characterization of an Alkaline Family I.4 Lipase from Bacillus sp. W130-35 Isolated from a Tidal Mud Flat with Broad Substrate Specificity  

Kim, Hee Jung (Department of Pharmacy, Sunchon National University)
Jung, Won Kyeong (Research Institute of Life Pharmaceutical Sciences, Sunchon National University)
Lee, Hyun Woo (Department of Pharmacy, Sunchon National University)
Yoo, Wanki (Department of Chemistry, Sookmyung Women's University)
Kim, T. Doohun (Department of Chemistry, Sookmyung Women's University)
Kim, Hoon (Department of Pharmacy, Sunchon National University)
Publication Information
Journal of Microbiology and Biotechnology / v.25, no.12, 2015 , pp. 2024-2033 More about this Journal
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℃. Its activity increased in the presence of 30% methanol and, remarkably, increased as well to 154.6% in the presence of Ca2+. Lip7-3 preferred p-nitrophenyl octanoate (C8) as a substrate and exhibited broad specificity for short- to long- chain 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.
Keywords
Bacillus sp. W130-35; broad substrate specificity; family I.4 lipase; methanol activation; tidal mud flat;
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