Stability and Catalytic Properties of Penicillin Acylase in Systems with Low Water Content

M. I. Youshko, A. V. Sinev, 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 9, 1999; Revision received April 23, 1999

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Stability and catalytic properties of native and immobilized penicillin acylase were studied in systems with low water content. Preparations of both native and immobilized penicillin acylase demonstrated the catalytic activity even in solid-phase systems which contained 3-5 wt. % of water. The stability and catalytic activity of penicillin acylase at low water content depended on the thermodynamic water activity (a_w) in the system.

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KEY WORDS: penicillin acylase, stability, solid-phase systems

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