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Influence of the Procedure to Immobilize Lipase on SBA-15 for Biodiesel Production from Palm Kernel Oil

Microbial lipase from Burkholderia cepacia was immobilized by covalent bond and physical adsorption on SBA-15 mesoporous support and its catalytic efficiency was measured in the formation of fatty acids ethyl esters from palm kernel oil. The immobilized biocatalyst and its support were characterized...

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Bibliographic Details
Published in:Catalysis letters 2021-08, Vol.151 (8), p.2187-2196
Main Authors: Pinto, Francisco G. H. S., Fernandes, Francisco R., Caldeira, Vinicius P. S., de Castro, Heizir F., Di Souza, Luiz, Santos, Anne G. D.
Format: Article
Language:English
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Summary:Microbial lipase from Burkholderia cepacia was immobilized by covalent bond and physical adsorption on SBA-15 mesoporous support and its catalytic efficiency was measured in the formation of fatty acids ethyl esters from palm kernel oil. The immobilized biocatalyst and its support were characterized by X-ray Diffraction, Fourier Transform Infrared Spectroscopy, N 2 Adsorption–desorption, and thermal analysis TG/DTG. The immobilization of the enzyme onto the support maintained the typical structure of the SBA-15. From the TG measurements, it can be deduced that about 25% of lipase was immobilized in SBA-15 via covalent bond and 15% was incorporated via physical adsorption. Both immobilized lipase preparations were used to perform the transesterification reactions using different oil: ethanol molar ratios and time. The biocatalyst prepared by physical adsorption promoted better results, measured by the apparent yield (> 90%) and conversion (98.9%) in all reactions, which were also confirmed by viscosity and density data. The regeneration of SBA-15 support was found to be feasible and demonstrated efficiency for 5 times, reducing the associated costs of the process. Graphic Abstract
ISSN:1011-372X
1572-879X
DOI:10.1007/s10562-020-03510-7