Isocyanate-mediated covalent immobilization of Mucor miehei lipase onto SBA-15 for transesterification reaction - Université de Lorraine Access content directly
Journal Articles Colloids and Surfaces B: Biointerfaces Year : 2013

Isocyanate-mediated covalent immobilization of Mucor miehei lipase onto SBA-15 for transesterification reaction

Abstract

Mucor miehei lipase (Mm-L) covalently bind on a hexagonally ordered silica SBA-15 (Santa Barbara Amorphous), previously functionalizecl with isocyanate moieties, was examined as biocatalyst for transesterification of colza oil wills methanol. The isocyanate-mesoporous silica (NCO-SBA-15) was obtained by condensation of silanol with triethoxysilane propyl isocyanate (TPI). The efficiency of the functionalization has been evidenced by infrared, Si-29 and C-13 NMR spectroscopies. The substrate provided a moderate hydrophobic microenvironment together with reactive sites for chemical immobilization of the enzyme. The biocatalyst containing 0.28 g of Mm-L per gram of support afforded a high level of transesterification activity (yield up to 80%) while using 1:1 molar ratio of methanol/colza oil and small amount of water. The biocatalyst showed higher operational stability than the corresponding physisorbed enzyme since it can be reused 6 times against 2 consecutive runs for the physisorbed enzyme.

Dates and versions

hal-01494100 , version 1 (22-03-2017)

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N. Canilho, J. Jacoby, Andreea Pasc, C. Carteret, F. Dupire, et al.. Isocyanate-mediated covalent immobilization of Mucor miehei lipase onto SBA-15 for transesterification reaction. Colloids and Surfaces B: Biointerfaces, 2013, 112, pp.139-145. ⟨10.1016/j.colsurfb.2013.07.024⟩. ⟨hal-01494100⟩
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