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Applied and Environmental Microbiology, April 2006, p. 2394-2399, Vol. 72, No. 4
0099-2240/06/$08.00+0 doi:10.1128/AEM.72.4.2394-2399.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Departments of Applied Life Science,1 Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto 860-0082, Japan,3 IMB Co., Ltd., Ooaza Hitotugi 1070-10, Amagi City, Fukuoka 838-0065, Japan2
Received 21 November 2005/ Accepted 24 January 2006
Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The Km and Vmax values for mono-2-ethylhexyl phthalate were 26.9 ± 4.3 µM and 18.1 ± 0.9 µmol/min · mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% homology with those of meta-cleavage hydrolases which are serine hydrolases but exhibited no significant homology with the sequences of serine esterases. The pentapeptide motif GXSXG, which is conserved in serine hydrolases, was present in the sequence. The enzymatic properties and features of the primary structure suggested that this enzyme is a novel enzyme belonging to an independent group of serine hydrolases.
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