A kinetic study of synthesis of amoxicillin using penicillin G acylase immobilized on agarose.
We present a kinetic model for the synthesis of amoxicillin from p-hydroxyphenylglycine methyl ester and 6-aminopenicillanic acid, catalyzed by penicillin G acylase immobilized on agarose, at 25 degrees C. Michaelis-Menten kinetic parameters (with and without inhibition) were obtained from initial velocity data (pH 7.5 and 6.5). Amoxicillin synthesis reactions were used to validate the kinetic model after checking mass transport effects. A reasonable representation of this system was achieved under some operational conditions, but the model failed under others. Nevertheless, it will be useful whenever a simplified model is required, e.g., in model-based control algorithms for the enzymatic reactor.
Gonçalves
L R
LR
Departamento de Engenharia Química, Universidade Federal do Ceará, Fortaleza, Brazil.
Fernandez-Lafuente
R
R
Guisán
J M
JM
Giordano
R L
RL
D000658:Amoxicillin / Q000138:chemical synthesis* / Q000378:metabolism*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli; D007700:Kinetics; D010397:Penicillanic Acid / Q000031:analogs & derivatives / Q000378:metabolism; D010399:Penicillin Amidase / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012685:Sepharose
D004800:Enzymes, Immobilized; D011994:Recombinant Proteins; D000658:Amoxicillin; D010397:Penicillanic Acid; D012685:Sepharose; D010399:Penicillin Amidase; C004408:aminopenicillanic acid