Abstract
The hydrophobicity of a support plays a critical role in the catalytic efficiency of immobilized lipases. 3-aminopropyltriethoxysilane (APTES)-modified silica clay (A-SC) was coupled with silane coupling agents of different alkyl chains (methyl triethoxysilane, vinyl triethoxysilane, octyl triethoxysilane, and dodecyl triethoxysilane) to prepare a series of hydrophobic support for lipase immobilization. The lipases were immobilized onto the support by conducting glutaraldehyde cross-linking processes. The results showed that the activity of the immobilized biocatalyst increased with hydrophobicity. The hydrolytic activity of Lip-Glu-C12-SC (contact angle 119.8°) can reach 5900 U/g, which was about three times that of Lip-Glu-A-SC (contact angle 46.5°). The immobilized lipase was applied as a biocatalyst for biodiesel production. The results showed that the catalytic yield of biodiesel with highly hydrophobic Lip-Glu-C12-SC could be as high as 96%, which is about 30% higher than that of Lip-Glu-A-SC. After being recycled five times, the immobilized lipase still maintained good catalytic activity and stability. This study provides a good strategy to improve the efficiency of immobilized lipases, showing great potential for future industrial application on biodiesel production.
Highlights
Received: 19 January 2022Lipases catalyze reactions such as the hydrolysis of triacylglycerol, esterification, transesterification, and interesterification
The results showed that the alkyl groups have been successfully introduced onto the silica clay
The results reveal that the hydrophobic microenvironment on the surface of immobilized lipase was destroyed by the presence of water, which reduces local hydrophobic interactions, in turn intensely affecting the catalytic efficiency of the immobilized lipase
Summary
Lipases (triacylglycerol hydrolase, E.C. 3.1.1.3) catalyze reactions such as the hydrolysis of triacylglycerol, esterification, transesterification, and interesterification They present high activity, good stability, unique selectivity, and specificity. In order to enhance its stability and reusability, lipases can be immobilized on various supports by techniques such as physical adsorption, embedding, covalent binding, and cross-linking [6,7,8,9]. These immobilization methods can perform the recovery and reuse of biocatalysts, control the loss of enzymes, reduce process costs, and improve its feasibility [10]. The effects of hydrophobicity of the support surface on the properties of the immobilized lipase and its performance on biodiesel production were investigated
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