Immobilization of penicillin G acylase on macro-mesoporous silica spheres.
In this study, macro-mesoporous silica spheres were prepared with a micro-device and used as the support for the immobilization of penicillin G acylase (PGA). To measure the enzymatic activity, the silica spheres with immobilized PGA were placed into a packed-bed reactor, in which the hydrolysis of penicillin G was carried out. The influences of the residence time, the initial concentration of the substrate, the accumulation of the target product 6-aminopenicillanic acid, and the enzyme loading amount on the performance of the immobilized PGA were investigated. The introduction of macropores increased the enzyme loading amount and decreased the internal mass transfer resistance, and the results showed that the enzyme loading amount reached 895 mg/g (dry support), and the apparent enzymatic activity achieved up to 1033 U/g (dry support). In addition, the immobilized PGA was found to have great stability.
The State Key Laboratory of Chemical Engineering, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China.
Junqi
J
Zhao
Yujun
Y
Wang
Guangsheng
G
Luo
Shenlin
S
Zhu
D000327:Adsorption / Q000187:drug effects; D055162:Biocatalysis / Q000187:drug effects; D001709:Biotechnology / Q000379:methods*; D004795:Enzyme Stability / Q000187:drug effects; D004800:Enzymes, Immobilized / Q000378:metabolism*; D008863:Microspheres; D009584:Nitrogen / Q000032:analysis; D010397:Penicillanic Acid / Q000031:analogs & derivatives / Q000378:metabolism; D010399:Penicillin Amidase / Q000378:metabolism*; D016062:Porosity / Q000187:drug effects; D012822:Silicon Dioxide / Q000494:pharmacology*; D013696:Temperature; D013997:Time Factors
D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D010397:Penicillanic Acid; D010399:Penicillin Amidase; D009584:Nitrogen; C004408:aminopenicillanic acid