无溶剂体系下表面活性剂修饰的猪胰脂酶催化酯交换反应的研究

Study on the interesterification catalyzed by surfactants modified porcine pancreas lipase in solvent free system

在水溶液中,采用Tween40、蔗糖酯S970、Span60三种表面活性剂修饰猪胰脂酶(porcine pancreas lipase,PPLipase);再以修饰的猪胰脂酶(Tween40-PPLipase、S970-PPLipase、Span60-PPLipase)为催化剂,在无溶剂体系中催化茶油与亚油酸酯交换反应。结果表明,在酶促反应达到平衡前,随着加酶量的增加酯交换量也随之增加;在相同的加酶量下,Tween40-PPLipase、S970-PPLipase和Span60-PPLipase催化酯交换的速率均高于PPLipase催化酯交换的速率;加酶量5%时,2h时PPLipase催化反应的酯交换量为16.1%,Tween40-PPLipase、Span60-PPLipase和S970-PPLipase催化反应的酯交换量分别为20.4%、21.1%和22.4%。达到平衡时,Tween40-PPLipase、Span60-PPLipase、S970-PPLipase和PPLipase催化反应的酯交换量基本相同,均为25%左右。

The porcine pancreas lipase （PPLipase） was modified by Tween40,Sucrose ester S970 and Span60 in aqueous solution,and then the Tween40-PPLipase,S970-PPLipase and Span60-PPLipase were used to catalyze the interesterification of camellia and linoleic acid in solvent free system. The results indicated that the acyl incorporation（la） was increased with the enzyme loading increasing before the reaction balance reached. The interesterification volecities of the reactions catalyzed by Tween40-PPLipase,Span60-PPLipase and S970-PPLipase were higher than that catalyzed by PPLipase when the enzyme Ioadings were same. At enzyme load 5% level,the la of the interesterifiecation catalyzed by PPLipase was 16.1% at 2h,however the las of the interesterification catalyzed by Tween40-PPLipase,Span60-PPLipase and S970-PPLipase were 20.4%, 21.1% and 22.4%,respectively. When the reaction balance reached,the las of the interesterifications catalyzed by Tween40-PPLipase, S970-PPLipase, Span60-PPLipase and PPLipase were same roughly, about 25%.