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Optimization of 6‐aminopenicillanic acid (6‐APA) production by using a new immobilized penicillin acylase
Author(s) -
TorresBacete Jesús,
Arroyo Miguel,
TorresGuzmán Raquel,
De La Mata Isabel,
Castillón María Pilar,
Acebal Carmen
Publication year - 2000
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20000042
Subject(s) - chemistry , hydrolysis , penicillin , substrate (aquarium) , enzyme , immobilized enzyme , chromatography , penicillin amidase , factorial experiment , covalent bond , organic chemistry , biochemistry , antibiotics , biology , ecology , statistics , mathematics
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 °C, whereas its soluble counterpart showed the same optimal pH value and a lower optimal temperature of 50 °C.