Application of cross-linked enzyme aggregates of Bacillus badius penicillin G acylase for the production of 6-aminopenicillanic acid.
OBJECTIVE
Optimization of 6-aminopenicillanic acid (6-APA) production using cross-linked enzyme aggregates (CLEA) of Bacillus badius penicillin G acylase (PAC).


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.


CONCLUSIONS
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.


CONCLUSIONS
The faster conversion of penicillin G to 6-APA by CLEA-PAC and efficient reusability holds a strong potential for the industrial application.
Rajendhran
J
J
Department of Genetics, Centre for Excellence in Genomic Sciences, School of Biological Sciences, Madurai Kamaraj University, Madurai, India.
Gunasekaran
P
P
D001407:Bacillus / Q000187:drug effects* / Q000201:enzymology; D003432:Cross-Linking Reagents / Q000737:chemistry; D004800:Enzymes, Immobilized / Q000737:chemistry*; D007218:Industrial Microbiology / Q000379:methods; D010397:Penicillanic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D010399:Penicillin Amidase / Q000378:metabolism / Q000494:pharmacology*
D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D010397:Penicillanic Acid; D010399:Penicillin Amidase; C004408:aminopenicillanic acid