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Journal of Biochemistry 2005 137(1):27-32; doi:10.1093/jb/mvi004
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© 2005 The Japanese Biochemical Society

BIOCHEMISTRY

Purification and Characterization of an Esterase Hydrolyzing Monoalkyl Phthalates from Micrococcus sp. YGJ1

Kiyofumi Maruyama*, Keiichi Akita, Chikako Naitou, Masahiko Yoshida and Toshiki Kitamura

Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu 501-1193

An esterase that specifically hydrolyzes medium-chain (C3–C5) 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, Hg2+, and Cu2+ 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.

* To whom correspondence should be addressed. Tel: +81-58-293-3061, Fax: +81-58-293-3061, E-mail: maruyama{at}cc.gifu-u.ac.jp


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