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

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, 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.Luiz Di Souza-In memoriam.

Valorization of Waste Cooking Oil into Biodiesel via Bacillus stratosphericus Lipase Amine-Functionalized Mesoporous SBA-15 Nanobiocatalyst

“…Moreover, according to Badiei et al [53] that would also indicate the occurrence of modifcation within the inner surface of the silica wall. Besides the homogenous distribution of the immobilized enzyme onto the SBA-15 surface and within its pores [36]. Not only that, but according to Kou et al [46] those results would also indicate entrapment of the enzyme molecules within the silica channels besides its surface adsorption onto the mesoporous 5(e)) confrmed the XRD-analysis as mentioned above and showed more observable arrangements of conservative mesoporous channels.…”

“…Upon functionalization, the capillary condensation shifted to lower P/P 0 , confrming shrinkage in pore diameter due to the presence of pendant organic moieties (-Si-CH 2 CH 2 CH 2 -NH 2 ), that further decreased upon the enzyme immobilization. Te desorption hysteresis loop likely became broader after enzyme immobilization, which might be attributed, according to Pinto et al [36]; to the presence of protein inside the pores, causing a delay in the nitrogen desorption. After introducing-Si-CH 2 CH 2 CH 2 -NH 2 and enzyme, the specifc surface area decreased from 802 m 2 /g for virgin SBA-15 to 612 and 579 m 2 /g, respectively.…”

“…Metal-impregnated SBA-15 has also been used for lipase immobilization for biodiesel production; for example, Pseudomonas fuorescens lipase immobilized over Camodifed mesoporous SBA-15 [33]. Moreover, Mucor miehei and Rhizopus oryzae lipases [34], Mucor miehei lipase [35], Candida rugosa lipase [21], and Burkholderia cepacia lipase 1 [36] immobilized on SBA-15 have also been reported for biodiesel production. Besides, other organic functionalized SBA-15, for example, Rhizomucor miehei lipase immobilized on aldehyde-functionalized SBA-15 [37], Candida antarctica, Termomyces lanuginosus, and Rhizomucor miehei lipases covalently immobilized on 3-glycidyloxypropyl trimethoxysilane modifed mesoporous SBA-15 [38], Actinomadura sediminis lipase immobilized on oleic acid modifed mesoporous SBA-15 [20], and porcine pancreatic lipase immobilized on mesoporous SBA-15/chitosan-glutaraldehyde matrix [39].…”