Moreno-Perez Sonia, Turati Daniela Flavia Machado, Borges Janaina Pires, Luna Pilar, Señorans Francisco Javier, Guisan Jose M, Fernandez-Lorente Gloria
Instituto de Catálisis, CSIC , Campus UAM-CSIC, 28049 Madrid, Spain.
Department of Biochemistry and Microbiology, Univ Estadual Paulista at Rio Claro - 8 UNESP , Rio Claro, SP 13506-900, Brazil.
J Agric Food Chem. 2017 Jan 11;65(1):117-122. doi: 10.1021/acs.jafc.6b05243. Epub 2016 Dec 21.
Different immobilized derivatives of two lipases were tested as catalysts of the synthesis of ethyl esters of omega-3 fatty acids during the ethanolysis of sardine oil in solvent-free systems at 25 °C. Lipases from Thermomyces lanuginosus (TLL) and Lecitase Ultra (a phospholipase with lipolytic activity) were studied. Lipases were adsorbed on hydrophobic Sepabeads C18 through the open active center and on an anion-exchanger Duolite with the active center exposed to the reaction medium. TLL-Sepabeads derivatives exhibit a high activity of 9 UI/mg of immobilized enzyme, and they are 20-fold more active than TLL-Duolite derivatives and almost 1000-fold more active than Lipozyme TL IM (the commercial derivative from Novozymes). Lecitase-Sepabeads exhibit a high selectivity for the synthesis of the ethyl ester of EPA that is 43-fold faster than the synthesis of the ethyl ester of DHA.
在25℃无溶剂体系中，将沙丁鱼油进行乙醇解反应时，测试了两种脂肪酶的不同固定化衍生物作为ω-3脂肪酸乙酯合成的催化剂。研究了来自嗜热栖热菌（TLL）的脂肪酶和Lecitase Ultra（一种具有脂解活性的磷脂酶）。脂肪酶通过开放的活性中心吸附在疏水性Sepabeads C18上，并通过暴露于反应介质的活性中心吸附在阴离子交换剂Duolite上。TLL-Sepabeads衍生物表现出9 UI/mg固定化酶的高活性，其活性比TLL-Duolite衍生物高20倍，比Lipozyme TL IM（诺维信的商业衍生物）高近1000倍。Lecitase-Sepabeads对EPA乙酯的合成表现出高选择性，其速度比DHA乙酯的合成快43倍。
