Abstract
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, N2 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.
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Authors are thankful to Conselho Nacional de Desenvolvimento Científico e Tecnológico CNPq (Process Number 448701/2018-6) and to CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior—Brazil)—Finance Code 001.
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Luiz Di Souza—In memoriam.
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Pinto, F.G.H.S., Fernandes, F.R., Caldeira, V.P.S. et al. Influence of the Procedure to Immobilize Lipase on SBA-15 for Biodiesel Production from Palm Kernel Oil. Catal Lett 151, 2187–2196 (2021). https://doi.org/10.1007/s10562-020-03510-7
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DOI: https://doi.org/10.1007/s10562-020-03510-7