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Functionalization of Mesoporous SBA-15 with APTES by Co-Condensation and its Effect on Immobilization of Candidarugosa Lipase

Functionalized SBA-15 with mesoscopic pore channels was synthesized by co-condensation of tetraethoxysilane and (3-aminopropyl) triethoxysilane (APTES) via hydrothermal process. Small-angle X-ray powder diffraction, scanning electron microscopy and transmission electron microscopy were used to monitor the effect of surface functionalization on the structural and textural features of the SBA-15. The results suggested that the structural ordering of functionalized SBA-15, as well as pore diameters, pore volumes and surface areas, were decreased with increasing the APTES molar ratio. Candida rugosa lipase (CRL) was used as a model enzyme for studying the effect of amino-functionalized on loading amount and enzymatic activity. The effects of pH and temperature on catalytic hydrolysis of tributyrin by immobilized CRL were investigated. The results showed that immobilized CRL had a well adaptability in a wide pH and temperature region, and CRL immobilized on functionalized SBA-15 exhibited much higher enzymatic activity than free CRL, especially, 5 mol% APTES functionalized SBA-15 immobilized CRL displayed the highest activity.