Immobilization of penicillin G acylase onto amino-modified silica hydrogel

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.

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