Application of cross‐linked enzyme aggregates of Bacillus badius penicillin G acylase for the production of 6‐aminopenicillanic acid

Aims:  Optimization of 6‐aminopenicillanic acid (6‐APA) production using cross‐linked enzyme aggregates (CLEA) of Bacillus badius penicillin G acylase (PAC). Methods and Results:  CLEA–PAC was prepared using purified/partially purified PAC with phenylacetic acid as active‐site blocking agent and glutaraldehyde as cross‐linker. Conversion of penicillin G to 6‐APA by CLEA–PAC was optimized using response surface methodology (RSM) (central composite rotatable design) consisting of a three‐factor–two‐level pattern with 20 experimental runs. Conclusion:  Nearly, 80% of immobilization yield was obtained when partially purified enzyme was used for the preparation of CLEA–PAC. Quantitative conversion of penicillin G to 6‐APA was observed within 60 min and the CLEA–PAC was reusable for 20 repeated cycles with 100% retention of enzyme activity. Significance and Impact of the Study:  The faster conversion of penicillin G to 6‐APA by CLEA–PAC and efficient reusability holds a strong potential for the industrial application.