Literature DB >> 11115389

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

J Torres-Bacete1, M Arroyo, R Torres-Guzmán, I de La Mata, M P Castillón, C Acebal.   

Abstract

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 2(3) 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 degrees C, whereas its soluble counterpart showed the same optimal pH value and a lower optimal temperature of 50 degrees C.

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Year:  2000        PMID: 11115389     DOI: 10.1042/ba20000042

Source DB:  PubMed          Journal:  Biotechnol Appl Biochem        ISSN: 0885-4513            Impact factor:   2.431


  1 in total

1.  Overexpression of penicillin V acylase from Streptomyces lavendulae and elucidation of its catalytic residues.

Authors:  Jesús Torres-Bacete; Daniel Hormigo; Raquel Torres-Gúzman; Miguel Arroyo; María Pilar Castillón; Luis José García; Carmen Acebal; Isabel de la Mata
Journal:  Appl Environ Microbiol       Date:  2015-02       Impact factor: 4.792

  1 in total

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