Immobilization of Lipases on Modified Silica Clay for Bio-Diesel Production: The Effect of Surface Hydrophobicity on Performance

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.

Enhanced Bioactivity of Enzyme/MOF Biocomposite via Host Framework Engineering

“…The selection of esterase is reasonable because it is an important hydrolase enzyme which can catalyze transesterification with a broad substrate range in organic solvent . Furthermore, there is a substantial documentation indicating that immobilization on a hydrophobic surface can activate esterase or lipase into its open-lid configuration, thereby exposing its catalytic active site to the surrounding environment for a more efficient biocatalytic reaction. − Given the hydrophobic properties of MAF-6, we hypothesized that the targeted esterase@MAF-6 would exhibit superior catalytic performance relative to free esterase.…”

Magnetic Iron Oxide Nanomaterials for Lipase Immobilization: Promising Industrial Catalysts for Biodiesel Production

“…These multi-point attachments enhance the rigidity of the lipase and protect the immobilized enzyme against external agents (heat, organic solvents, etc.). Additionally, there can be a combination of these four immobilization methods to enhance enzyme loading and stability [83], which eventually results in improving catalytic performance. Finally, it is worth mentioning that for all these immobilization methods, the reaction conditions should be optimized in terms of pH, immobilization time, temperature, lipase concentration and enzyme/support ratio.…”

Ultrasound-assisted intensification of Pickering interfacial biocatalysis preparation of vitamin A aliphatic esters

“…Hence, hydrophobic groups, such as butyl groups, octyl groups, dodecyl groups, phenyl groups, and octadecyl groups, have been comprehensively employed to upgrade the desired microenvironment properties for enzymes [29] . Under certain circumstances, the enzymes immobilized by this approach may be released into the medium, resulting in an activation decrease and contaminating the product [30] . In addition, while there has been considerable research on understanding the hydrophobicity modification and the performance of the immobilized lipase, there is limited knowledge on the impact of introducing modified functional groups with hydrophilicity and hydrophobicity simultaneously on the properties of immobilized enzymes.…”