Department of Chemical and Food Engineering, UFSC, Florianópolis, SC, 88040-900, Brazil.
Departamento de Biocatálisis, Instituto de Catálisis (CSIC),, UAM, Cantoblanco, 28049, Madrid, Spain.
Appl Biochem Biotechnol. 2018 Jul;185(3):705-716. doi: 10.1007/s12010-017-2683-1. Epub 2018 Jan 3.
The performance of two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 immobilized in different supports was investigated. The two lipases were adsorbed on four different hydrophobic supports. Interesting results were obtained for both lipases and for the four supports. However, the most active derivative was prepared by immobilization of Eversa® Transform 2.0 on Sepabeads C-18. Ninety-nine percent of fatty acid ethyl ester was obtained, in 3 h at 40 °C, by using hexane as solvent, a molar ratio of 4:1 (ethanol/oil), and 10 wt% of immobilized biocatalyst. The final reaction mixture contained traces of monoacylglycerols but was completely free of diacylglycerols. After four reaction cycles, the immobilized biocatalyst preserved 75% of activity. Both lipases immobilized in Sepabeads C-18 were very active with ethanol and methanol as acceptors, but they were much more stable in the presence of ethanol.
研究了两种新型商业廉价脂肪酶 Eversa® Transform 和 Eversa® Transform 2.0 在不同载体上的固定化性能。这两种脂肪酶被吸附在四种不同的疏水载体上。两种脂肪酶和四种载体都得到了有趣的结果。然而,通过将 Eversa® Transform 2.0 固定在 Sepabeads C-18 上制备了最活性的衍生物。在 40°C 下,使用正己烷作为溶剂,摩尔比为 4:1(乙醇/油),以及 10wt%的固定化生物催化剂,99%的脂肪酸乙酯在 3 小时内得到。最终的反应混合物含有痕量的单酰基甘油,但完全不含二酰基甘油。经过四个反应循环,固定化生物催化剂保持了 75%的活性。两种固定在 Sepabeads C-18 上的脂肪酶都具有很强的乙醇和甲醇接受能力,但在乙醇存在下更稳定。