Outperformance in Acrylation: Supported D-Glucose-Based Ionic Liquid Phase on MWCNTs for Immobilized Lipase B from Candida antarctica as Catalytic System

This study presents a highly efficient method of a synthesis of n -butyl acrylate via esterification of acrylic acid and n -butanol in the presence of supported ionic liquid phase (SILP) biocatalyst consisting of the lipase B from Candida antarctica (CALB) and multi-walled carbon nanotubes (MWCNTs)...

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Bibliographic Details
Published in:Materials
Main Authors: Anna Szelwicka, Karol Erfurt, Sebastian Jurczyk, Slawomir Boncel, Anna Chrobok
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2021
Subjects:
alkyl acrylates
esterification
biocatalysis
supported ionic liquid phase
lipases
Technology
T
Electrical engineering. Electronics. Nuclear engineering
TK1-9971
Engineering (General). Civil engineering (General)
TA1-2040
Microscopy
QH201-278.5
Descriptive and experimental mechanics
QC120-168.85
Antarc*
Antarctica
Online Access:https://doi.org/10.3390/ma14113090
https://doaj.org/article/81f1922c4fb1413d89f13ac1bf5fd148
Description
Summary:This study presents a highly efficient method of a synthesis of n -butyl acrylate via esterification of acrylic acid and n -butanol in the presence of supported ionic liquid phase (SILP) biocatalyst consisting of the lipase B from Candida antarctica (CALB) and multi-walled carbon nanotubes (MWCNTs) modified by D-glucose-based ionic liquids. Favorable reaction conditions (acrylic acid: n -butanol molar ratio 1:2, cyclohexane as a solvent, biocatalyst 0.150 g per 1 mmol of acrylic acid, temperature 25 °C) allowed the achievement of a 99% yield of n -butyl acrylate in 24 h. Screening of various ionic liquids showed that the most promising result was obtained if N -(6-deoxy-1- O -methoxy-α-D-glucopyranosyl)- N , N , N -trimethylammonium bis-(trifluoromethylsulfonyl)imide ([N(CH 3 ) 3 GlcOCH 3 ][N(Tf) 2 ]) was selected in order to modify the outer surface of MWCNTs. The final SILP biocatalyst–CNTs-[N(CH 3 ) 3 GlcOCH 3 ][N(Tf) 2 ]-CALB contained 1.8 wt.% of IL and 4.2 wt.% of CALB. Application of the SILP biocatalyst led to the enhanced activity of CALB in comparison with the biocatalyst prepared via physical adsorption of CALB onto MWCNTs (CNTs-CALB), as well as with commercially available Novozyme 435. Thus, the crucial role of IL in the stabilization of biocatalysts was clearly demonstrated. In addition, a significant stability of the developed biocatalytic system was confirmed (three runs with a yield of ester over 90%).

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