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Abstract: Mucor miehei lipase (Mm-L) covalently bind on a hexagonally ordered silica SBA-15 (Santa Barbara Amorphous), previously functionalized with isocyanate moieties, was examined as biocatalyst for transesterification of colza oil with 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, 29Si and 13C 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. [Copyright &y& Elsevier]

Highlights: [•] Physisorption of Mucor Miehei Lipase onto ordered mesoporous silica. [•] High wall thickness is required to protect the support upon enzyme adsorption. [•] Mucor Miehei Lipase adsorption follows Langmuir isotherm. [•] Biocatalyst used for the methanolysis of colza in the absence of nonpolar solvents. [•] Good transesterification yields obtained by the addition of small amounts of water. [ABSTRACT FROM AUTHOR]