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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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Published in: | Catalysis letters 2021-08, Vol.151 (8), p.2187-2196 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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 |
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ISSN: | 1011-372X 1572-879X |
DOI: | 10.1007/s10562-020-03510-7 |