Immobilization of penicillin G acylase onto amino-modified
silica hydrogel
Immobilization of penicillin G acylase onto amino-modified
silica hydrogel
Weibing Dong,Huining HE,Junbo Gong,Victor C. YANG,
Tianjin Key Laboratory
for Modern Drug Delivery and High Efficiency, School of Chemical Engineering
and Technology, Tianjin University, Tianjin 300072, China;
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±0.17nm. 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 2.5h. This sol-gel preparation is simple and shows prominent potential value in industrial processing.
出版日期: 2010-03-05
引用本文:
. Immobilization of penicillin G acylase onto amino-modified
silica hydrogel[J]. Front. Chem. Sci. Eng., 2010, 4(1): 87-90.
Weibing Dong, Huining HE, Junbo Gong, Victor C. YANG, . Immobilization of penicillin G acylase onto amino-modified
silica hydrogel. Front. Chem. Sci. Eng., 2010, 4(1): 87-90.
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