Abstract
A modified model was proposed for the pH-inactivation rate constant of penicillin G acylase obtained from various species of Escherichia coli. A new approach was applied and a new parameter called steric factor defined to obtain the more precise description of the pH-inactivation rate constant. The parameter is used as the measure of the conformational rigidity of the enzyme with respect to pH. The proposed model accuracy was verified and compared with the reported models. The model can be used for pH-inactivation studies of other biocatalysts by determining its parameters. Also, the effect of the ionic strength on the stability of the enzymatic solution of penicillin G acylase has been studied in NaCl and KCl solution. The inactivation reaction of the enzyme with respect to the ionic strength of the solution obeys first order irreversible mechanism. The rate constant of this reaction was determined as a function of the solution ionic strength and a mathematical description was developed. The results show the role of the ionic strength of the non-inhibitory salt solution on the stability of penicillin G acylase, especially for long-time storage and operation.
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