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Optimization of 6-aminopenicillanic acid (6-APA) production by using a new immobilized penicillin acylase
Article first published online: 23 DEC 2010
2000 International Union of Biochemistry and Molecular Biology
Biotechnology and Applied Biochemistry
Volume 32, Issue 3, pages 173–177, December 2000
How to Cite
Torres-Bacete, J., Arroyo, M., Torres-Guzmán, R., De La Mata, I., Castillón, M. P. and Acebal, C. (2000), Optimization of 6-aminopenicillanic acid (6-APA) production by using a new immobilized penicillin acylase. Biotechnology and Applied Biochemistry, 32: 173–177. doi: 10.1042/BA20000042
- Issue published online: 23 DEC 2010
- Article first published online: 23 DEC 2010
- Received 22 May 2000/11 September 2000; accepted 18 September 2000
- Eupergit C;
- factorial design;
- Streptomyces lavendulae
A new immobilized penicillin acylase (ECPVA) was obtained by covalent binding of penicillin acylase from Streptomyces lavendulae on Eupergit C. Enzymic hydrolysis of penicillin V catalysed by ECPVA was optimized using a 23 factorial design of experiments, and the selected parameters for this study were pH, temperature and substrate concentration. The immobilized enzyme showed an optimal pH value of 9.5–10.5, and an optimal temperature of 60 °C, whereas its soluble counterpart showed the same optimal pH value and a lower optimal temperature of 50 °C.