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Purification and characterization of an esterase hydrolyzing monoalkyl phthalates from Micrococcus sp. YGJ1.

Abstract：

:An esterase that specifically hydrolyzes medium-chain (C(3)-C(5)) monoalkyl phthalates was purified from phthalate-grown Micrococcus sp. YGJ1. The enzyme activity was split into two fractions by hydrophobic chromatography on Phenyl Sepharose, and the enzymes were purified to homogeneity from each fraction. The purified enzymes showed similar properties with respect to molecular mass (60 kDa), subunit molecular mass (27 kDa), N-terminal amino acid sequence, optimal pH (about 7.5), temperature-dependence, substrate specificity, and inhibitor susceptibility. The enzymes showed no activity toward various dialkyl phthalates or aliphatic carboxyl esters. 2-Mercaptoethanol effectively protected the enzymes from spontaneous inactivation. Diethylpyrocarbonate, p-chloromercuribenzoate, Hg(2+), and Cu(2+) strongly inhibited the enzymes, while phenylmethylsulfonyl fluoride produced weak inhibition, and various metal chelating reagents were ineffective. These findings show that the enzymes bear a close resemblance to the putative phthalate ester hydrolase (PehA) of Arthrobacter keyseri 12B.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Maruyama K,Akita K,Naitou C,Yoshida M,Kitamura T

doi

10.1093/jb/mvi004

keywords:

subject

Has Abstract

pub_date

2005-01-01 00:00:00

pages

27-32

issue

1

eissn

0021-924X

issn

1756-2651

pii

137/1/27

journal_volume

137

pub_type

杂志文章

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