Frontiers of Chemical Science and Engineering
>> 2010,
Volume 4,
Issue 1
doi:
10.1007/s11705-009-0298-y
Research articles
Immobilization of penicillin G acylase onto amino-modified
silica hydrogel
Tianjin Key Laboratory
for Modern Drug Delivery and High Efficiency, School of Chemical Engineering
and Technology, Tianjin University, Tianjin 300072, China; |
Available online: 2010-03-05
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Abstract
Amino-modified silica hydrogel (N-MSHG) was prepared by a simple sol-gel processing via the co-condensation of commercial silica sol with 3-aminopropyltrie-oxysilane. Penicillin G acylase (PGA), a model enzyme, was covalently immobilized onto the N-MSHG and then was used for the enzymatic synthesis of amoxicillin. The samples were characterized by Nitrogen sorption analysis, FT-IR and thermal gravimetric analysis (TGA). The results showed that the amino-modified gel was a mesoporous material with an average pore size of 12.64±0.17nm. The immobilization process was efficient and the immobilized enzyme showed high catalytic efficiency. The yield of the synthesis of amoxicillin in aqueous media was 38% for 2.5h. This sol-gel preparation is simple and shows prominent potential value in industrial processing.