Activity of Penicillin Acylase from E. coli in the Reversed-Micelle System AOT--H₂O--Octane

T. A. Shamolina, V. A. Drachev, and V. K. Svedas^*

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-3181; E-mail: vytas@enzyme.genebee.msu.su

^* To whom correspondence should be addressed.

Received April 16, 1999

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The behavior of a penicillin acylase from E. coli was studied in the reversed-micelle system AOT--H₂O--octane. Kinetic studies of the enzymatic hydrolysis of the m-carboxy-p-nitroanilide of phenylacetic acid, titration of the penicillin acylase active site with an irreversible specific inhibitor (phenylmethylsulfonyl fluoride), sedimentation analysis at different hydration degrees, and chemical modification showed that the enzyme loses no more than 20% of its initial activity during 3-4 h in the reversed-micelle systems of different hydration degrees and retains its catalytically active structure.

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KEY WORDS: penicillin acylase, heterodimer, reversed micelles, subunit composition

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