4.7 Article

Covalent immobilization of lipase from Candida rugosa on epoxy-activated cloisite 30B as a new heterofunctional carrier and its application in the synthesis of banana flavor and production of biodiesel

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 178, Issue -, Pages 569-579

Publisher

ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.02.146

Keywords

Heterofunctional carrier; Lipase immobilization; Activated cloisite; Esterification; Transesterification

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In this study, a new heterofunctional carrier ECL was prepared and successfully utilized for the immobilization of lipase LECL, showing excellent catalytic performance and thermal stability. The research provides a new approach for the development of biocatalysis field.
In this paper, an epoxy-activated cloisite (ECL) was prepared as a new heterofunctional carrier via a reaction be-tween cloisite 30B (CL) and epichlorohydrin and utilized for covalent immobilization of lipase from Candida rugosa. The lipase immobilized on the ECL (LECL) was successfully used in the olive oil hydrolysis, synthesis of isoamyl acetate (banana flavor), and biodiesel production. The TGA, FT-IR, SEM, and XRD were used to character-ize CL, ECL, and LECL. The influences of temperature, pH, thermal stability, and storage capacity were examined in the olive oil hydrolysis. The effects of solvent, temperature, time, water content, and substrates molar ratio on the yields of ester and biodiesel were also investigated. In the optimized conditions, the hydrolytic activity of LECL was 1.85 +/- 0.05 U/ mg, and the maximum yield of ester and biodiesel was 91.6% and 95.4%, respectively. The LECL showed good thermal stability and storage capacity compared to the free lipase. Additionally, LECL was re-usable for both esterification and transesterification after being used for nine cycles. (c) 2021 Elsevier B.V. All rights reserved.

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