A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp GMD509 SCIE SCOPUS

Cited 26 time in WEB OF SCIENCE Cited 28 time in Scopus
Title
A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp GMD509
Author(s)
Park, Sang-Yi; Kim, Jun-Tae; Kang, Sung Gyun; Woo, Jung-Hee; Lee, Jung-Hyun; Choi, Hyoung-Tae; Kim, Sang-Jin
KIOST Author(s)
Kang, Sung Gyun(강성균)Lee, Jung Hyun(이정현)
Publication Year
2007-11
Abstract
Vibrio sp. GMD509, a marine bacterium isolated from eggs of the sea hare, exhibited lipolytic activity on tributyrin (TBN) plate, and the gene representing lipolytic activity was cloned. As a result, an open reading frame (ORF) consisting of 1,017 bp (338 aa) was found, and the deduced amino acid sequence of the ORF showed low similarity (< 20%) to alpha/beta hydrolases such as dienelactone hydrolases and esterase/lipase with G-X-1-S-X-2-G sequence conserved. Phylogenetic analysis suggested that the protein belonged to a new family of esterase/lipase together with various hypothetical proteins. The enzyme was overexpressed in Escherichia coli and purified to homogeneity. The purified enzyme (Vlip509) showed the best hydrolyzing activity toward p-nitrophenyl butyrate (C-4) among various p-nitrophenyl esters (C-2 to C-18), and optimal activity of Vlip509 occurred at 30 degrees C and pH 8.5, respectively. Kinetic parameters toward p-nitrophenyl butyrate were determined as K (m) (307 mu M), k(cat) (5.72 s(-1)), and k(cat)/K-m (18.61 s(-1) mM(-1)). Furthermore, Vlip509 preferentially hydrolyzed the S-enantiomer of racemic ofloxacin ester. Despite its sequence homology to dienelactone hydrolase, Vlip509 showed no dienelactone hydrolase activity. This study represents the identification of a novel lipolytic enzyme from marine environment.
ISSN
0175-7598
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4624
DOI
10.1007/s00253-007-1134-2
Bibliographic Citation
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.77, no.1, pp.107 - 115, 2007
Publisher
SPRINGER
Subject
THERMOSTABLE ESTERASE; SEQUENCE SIMILARITY; METAGENOMIC LIBRARY; LIPASE; BIOCATALYSIS; PURIFICATION; ENZYMES; CLONING; CLASSIFICATION; ALIGNMENT
Keywords
screening; lipase/esterase; dienelactone hydrolase; Vibrio; marine microorganism
Type
Article
Language
English
Document Type
Article
Publisher
SPRINGER
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