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A. V. Stepashkina, A. S. Yasnaya, A. I. Berezin, V. I. Tishkov

Influence of pH On thermal stability of penicillin acylase from Alcaligenes faecalis

Abstract

Penicillin G acylase (PA, EC 3.5.1.11) from Alcaligenes faecalis (AfPA) is one of the most thermostable bacterial penicillin acylases. However the systematic data about thermal stability of AfPA are not presented in literature. Systematic study of influence of pH on thermal stability of AfPA was done in pH range 7.5–9.5. It was found that in all pH range studied enzyme inactivation follows the first order kinetics. Dependence of inactivation rate constant on pH has S-shape with inflection point at pH 8.3–8.5. Temperature dependences of inactivation rate constant at four pH were obtained and activation parameters DH# and DS# were calculated for each pH value. Decrease of both values, DH# and DS#, with pH growth shows that minimum one iogenic group is essential for the enzyme thermal stability.
Moscow University Chemistry Bulletin.
2010, Vol. 51, No. 3, P. 164
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
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