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. Graphic Abstract

中文翻译：

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固定脂肪酶的程序对 SBA-15 的影响，用于从棕榈仁油生产生物柴油

摘要 洋葱伯克霍尔德菌的微生物脂肪酶通过共价键和物理吸附固定在 SBA-15 介孔载体上，并测定了其在棕榈仁油脂肪酸乙酯形成过程中的催化效率。固定化生物催化剂及其载体通过 X 射线衍射、傅里叶变换红外光谱、N 2 吸附-解吸和热分析 TG/DTG 进行表征。酶在载体上的固定保持了 SBA-15 的典型结构。从 TG 测量可以推断，大约 25% 的脂肪酶通过共价键固定在 SBA-15 中，15% 通过物理吸附结合。两种固定化脂肪酶制剂都用于使用不同的油：乙醇摩尔比和时间进行酯交换反应。通过物理吸附制备的生物催化剂促进了更好的结果，通过所有反应的表观产率 (> 90%) 和转化率 (98.9%) 来衡量，这也得到了粘度和密度数据的证实。发现 SBA-15 载体的再生是可行的，效率提高了 5 倍，从而降低了该过程的相关成本。图形摘要