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Immobilization of penicillin G acylase onto amino-modified silica hydrogel

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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-aminopropyltrieoxysilane. 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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Authors and Affiliations

  1. Tianjin Key Laboratory for Modern Drug Delivery and High Efficiency, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China

    Weibing Dong, Huining He, Junbo Gong & Victor C. Yang

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  1. Weibing Dong
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  2. Huining He
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  3. Junbo Gong
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  4. Victor C. Yang
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Correspondence to Junbo Gong.

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Dong, W., He, H., Gong, J. et al. Immobilization of penicillin G acylase onto amino-modified silica hydrogel. Front. Chem. Eng. China 4, 87–90 (2010). https://doi.org/10.1007/s11705-009-0298-y

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  • DOI: https://doi.org/10.1007/s11705-009-0298-y

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