Candida rugosa lipase immobilized on hydrophobic support Accurel MP 1000 in the synthesis of emollient esters.

Luiz Henrique Sales De Menezes,Marta Maria Oliveira Dos Santos,Adriano Aguiar Mendes,Julieta Rangel De Oliveira,Marcelo Franco,Eliezer Luz Do Espírito Santo,Iasnaia Maria De Carvalho Tavares

doi:10.1007/s10529-021-03196-w

Abstract

To immobilize Candida rugosa lipase in Accurel MP 1000 (CRL-AMP) by physical adsorption in organic medium and apply in the synthesis of wax esters dodecanoyl octadecanoate 1 and hexadecanoyl octadecanoate 2 in a heptane medium, as well as evaluating the stability and recyclability of CRL-AMP in six reaction cycles. The specific activity (Asp) for CRL-AMP was 200 ± 20 U mg-1. Its catalytic activity was 1300 ± 100 U g-1. CRL-AMP was used in the synthesis of esters in heptane medium with a 1:1 acid:alcohol molar ratio at 45°C and 200rpm. In synthesis 1, conversion was 62.5 ± 3.9% in 30min at 10% m v-1 and 56.9 ± 2.8% in 54min at 5% m v-1; while in synthesis 2, conversion was 79.0 ± 3.9% in 24min at 10% m v-1, and 46.0 ± 2.4% in 54min at 5% m v-1. Reuse tests after six consecutive cycles of reaction showed that the biocatalyst retained approximately 50% of its original activity for both reaction systems. CRL-AMP showed a high potential in the production of wax esters, since it started from low enzymatic load and high specific activities and conversions were obtained, in addition to allowing an increase in stability and recyclability of the prepared biocatalyst.

Highlights

Emollient esters are long chain organic compounds with high molecular weight, formed by long chain alcohols and carboxylic acids (Serrano-Arnaldos et al, 2016)
The catalytic properties of the prepared Candida rugosa lipase (CRL)-Accurel MP 1000 (AMP) were determined after quantification of the hydrolytic activity (HA) in free and immobilized lipase to determine the catalytic activity of the immobilized enzyme, whose observed HA values were 8917.57 ± 249.29 U g-1 and 1300 ± 100 U g-1, respectively
This reduction indicates that the lipase molecules are not accessible to the drops of olive oil and the immobilization of CRL occurred in the internal part of the AMP, because CRL is a globular protein with molecular size of 50Å × 42Å × 33Å (Gao et al, 2010) and molecular diameter of near 0.5 nm (much smaller than the average diameter of the AMP pores, 25 nm (Sabbani et al, 2006))

Summary

Introduction

Emollient esters are long chain organic compounds (from 12 carbon atoms) with high molecular weight, formed by long chain alcohols and carboxylic acids (Serrano-Arnaldos et al, 2016). These esters are neither toxic nor greasy (Khan et al, 2015), they are classified as fine chemical products (Rani et al., 2015) and are commonly used in the cosmetic, pharmaceutical and lubricant industries (Lima et al, 2018; Miguez et al, 2018). Wax ester synthesis reactions are usually catalyzed by toxic and corrosive chemical compounds such as hydrofluoric acid and sulfuric acid (Esfandmaz et al, 2018). The enzymatic route has proved attractive for the production of these esters because it is a process with low energy consumption, high productivity, and good stability compared to organic solvents (Bandikari et al, 2018), in addition to having broad substrate specificity and exhibiting high enantioselectivity (Benamia et al, 2016)

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