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Biotechnology and Applied Biochemistry (2000) 32, (173–177) (Printed in Great Britain)

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Optimization of 6-aminopenicillanic acid (6-APA) production by using a new immobilized penicillin acylase

Jesús Torres-Bacete, Miguel Arroyo¹, Raquel Torres-Guzmán, Isabel de la Mata, María Pilar Castillón and Carmen Acebal

Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad Complutense de Madrid, 28040 Madrid, Spain

Abbreviations used: 6-APA, 6-aminopenicillanic acid; PDAB, p-dimethyl-aminobenzaldehyde; IU, international unit.

¹ To whom correspondence should be addressed (e-mail arroyo@solea.quim.ucm.es).

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.

Received 22 May 2000/11 September 2000; accepted 18 September 2000

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