Improvement strategy for operational stability of penicillin acylase for 6-APA production

Abstract

An indigenous Escherichia coli ATCC 11105 was selected for the study of 6-APA production and penicillin acylase enzyme operational stability. To optimize the different process parameters such as pH, temperature, substrate concentration, and cell lysis for 6-APA production intensive studies were carried out. In batch mode complex media was used to achieve maximum production of penicillin acylase enzyme with high potency. To protect the enzyme's operational stability, the enzyme was cross-linked with carbohydrate based polymers namely agar and agarose. The enzyme activity was found to be optimum at temperature 37° C and pH 8. Immobilized enzyme showed higher temperature and pH stability than the native enzyme. Higher half life for enzyme inactivation (increased stability) was observed for modified penicillin acylase above 40° C and pH range of 2-10.