Immobilization of penicillin G acylase on macro-mesoporous silica spheres

• Published in: Bioresource technology Vol. 102; no. 2; pp. 529 - 535
• Main Authors: Zhao, Junqi, Wang, Yujun, Luo, Guangsheng, Zhu, Shenlin
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 2011; [New York, NY]: Elsevier Ltd; Elsevier
• Subjects: Adsorption - drug effects; Biocatalysis - drug effects; Biological and medical sciences; Biotechnology; Biotechnology - methods; Drying; Enzyme immobilization; Enzyme Stability - drug effects; Enzymes; Enzymes, Immobilized - metabolism; Fundamental and applied biological sciences. Psychology; Immobilization; Immobilization of enzymes and other molecules; Immobilization techniques; Macropore; Mass transfer; Mass transfer resistance; Mesopore; Methods. Procedures. Technologies; Microspheres; Nitrogen - analysis; Penicillanic Acid - analogs & derivatives; Penicillanic Acid - metabolism; Penicillin Amidase - metabolism; Penicillin G; Penicillin G acylase; Porosity - drug effects; Reactors; Silicon dioxide; Silicon Dioxide - pharmacology; Temperature; Time Factors; Uranium; Enzyme immobilization; Mesopore; Mass transfer resistance; Penicillin G acylase; Macropore; Enzyme; Amidase; Immobilization; Benzylpenicillin; Silica; Mesoporosity; Mass transfer; Inorganic compound; Hydrolases; Immobilized enzyme; Transfer resistance; Macroporosity
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2010.09.076

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.