Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free

Daniela Remonatto,Jorge Ninow,Débora Oliveira,J. Vladimir Oliveira,J. Manuel Guisan,Gloria Fernandez-Lorente

doi:10.1007/s12010-021-03774-8

Daniela Remonatto, Jorge Ninow + Show 4 more

Open Access

https://doi.org/10.1007/s12010-021-03774-8

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Abstract

Lipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immobilized lipases was investigated in the transesterification of sunflower oil solvent-free in an anhydrous medium. Interesting results were obtained for both lipases and the four supports, but with Sepabeads support the lipases Eversa showed high catalytic activity. However, the more stable and efficient derivative was Eversa® Transform immobilized on Sepabeads C-18. A 98 wt% of ethyl ester of fatty acid (FAEE) was obtained, in 3 h at 40ºC, ethanol/sunflower oil molar ratio of 3:1 and a 10 wt% of the immobilized biocatalyst. After 6 reaction cycles, the immobilized biocatalyst preserved 70 wt% of activity. Both lipases immobilized in Sepabeads C-18 were highly active and stable in the presence of ethanol. The immobilization of Eversa Transform and Eversa Transform 2.0 in hydrophobic supports described in this study appears to be a promising alternative to the immobilization and application of these news lipases still unexplored.

Highlights

Lipases are biocatalysts naturally robust and efficient, can be used for the production of many different molecules, and have a wide range of industrial applications thanks to their broad specificity and commercial accessibility [1,2,3]
The lipases were immobilized by interfacial adsorption on four hydrophobic supports with different characteristics Sepabeads-C18, Lewatit-DVB, Purolite-C18, and PuroliteDVB
In the immobilization of soluble lipases Eversa Transform and Eversa Transform 2.0, by simple interfacial adsorption on four hydrophobic supports Purolite C18, Purolite-DVB, Lewatit-DVB, and Sepabeads-C18 support had immobilization yield was higher than 95 wt%

Summary

Introduction

Lipases (triacylglycerol acyl- hydrolase, EC 3.1.1.3) are biocatalysts naturally robust and efficient, can be used for the production of many different molecules, and have a wide range of industrial applications thanks to their broad specificity and commercial accessibility [1,2,3]. Among these molecules of interest is ethyl oleate, which is an ester with applications in cosmetics, in the food industry and in the production of biofuels as biodiesel [4,5,6]. There are very few studies into the immobilization of Eversa lipases which is still a field to be better explored [13,14,15]

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