REGULATION OF THE SUPRAMOLECULAR STRUCTURE AND THE CATALYTIC ACTIVITY OF PENICILLIN ACYLASE FROM ESCHERICHIA-COLI IN THE SYSTEM OF REVERSED MICELLES OF AEROSOL OT IN OCTANEстатья
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Аннотация:The properties of penicillin acylase from E. coli solubilized by hydrated reversed micelles (RM) of Aerosol OT in octane were studied. The dependence of catalytic activity on the hydration degree, a parameter which determines the size of the micelle inner cavity, has a curve with three optima, each one corresponding to the enzyme functioning either in a dimer form (w(o) = 23) or in a form of separate subunits, a heavy one, beta, and a light one, alpha (w(o) = 20 and 14, respectively). The reversible dissociation of the enzyme was confirmed by ultracentrifugation followed by electrophoresis.