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Application of cross‐linked enzyme aggregates of Bacillus badius penicillin G acylase for the production of 6‐aminopenicillanic acid
Author(s) -
Rajendhran J.,
Gunasekaran P.
Publication year - 2007
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.2006.02043.x
Subject(s) - chemistry , penicillin , glutaraldehyde , penicillin amidase , enzyme , phenylacetic acid , central composite design , response surface methodology , chromatography , biochemistry , antibiotics
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.