Immobilization of Trypsin on Amino Acid-modified SiO2 Porous Materials

Abstract

Abstract: To improve the biocompatibility and hydrophobicity of silica carrier material, and maintain the biological activity of embedded biological molecules, the synthetic routes of hydrolysis precursor 3-aminopropyl trimethoxysilane modified by amino acids are reported. The SiO2 porous material precursor modified by amino acid was prepared by a acryl chloride method. To be specific, the N-(9-Fluorenylmethoxycarbonyl)-L-valine reacted with thionyl chloride. The obtained compounds further react 3-aminopropyl trimethoxysilane. The valine modified precursor is obtained after removaling Fomc group. All obtained compounds were characterized by IR、MS、1H-NMR.. Using amino acids modified APTMS for silicon source, immobilized trypsin was prepared on a mild sol-gel process. When the molar ratio of amino acid modified 3-aminopropyl trimethoxysilane in hydrolysis precursor was 15 mol%, the immobilized trypsin shows the highest activity. The enzyme activity of immobilized trypsin by amino acid modified 3-aminopropyl trimethoxysilane is 2 times of that of free enzyme. The enzyme activity of immobilized trypsin by hybrid materials is 5 times of that of enzyme immobilized by tetramethoxysilane. The synthesized hybrid materials show a good biocompatibility.

Key words: silica, enzyme activity, amino acid, trypsin

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LI Ye*, ZHANG Heng-Jian, LIAO Ming-Xia, LIU Tao. Immobilization of Trypsin on Amino Acid-modified SiO₂ Porous Materials[J]. Chem. J. Chinese Universities, 2011, 32(5): 1100.

References

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Immobilization of Trypsin on Amino Acid-modified SiO₂ Porous Materials

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