Optimization of 6-aminopenicillanic acid (6-APA) production by using a new immobilized penicillin acylase.
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.
Torres-Bacete
J
J
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad Complutense de Madrid, 28040 Madrid, Spain.
Arroyo
M
M
Torres-Guzmán
R
R
de La Mata
I
I
Castillón
M P
MP
Acebal
C
C
D004800:Enzymes, Immobilized / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010397:Penicillanic Acid / Q000031:analogs & derivatives* / Q000191:economics / Q000302:isolation & purification / Q000378:metabolism; D010399:Penicillin Amidase / Q000378:metabolism*; D010404:Penicillin V / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology; D013696:Temperature
D004800:Enzymes, Immobilized; D010397:Penicillanic Acid; D010399:Penicillin Amidase; C004408:aminopenicillanic acid; D010404:Penicillin V