单-(2-O-乙烯癸二酰)-β-环糊精的酶促合成和结构分析  

Enzymatic synthesis and structure analysis of the monosubstituted derivative of β-cyclomaltoheptaose

作　　者：肖咏梅[1] 吴起[1] 王娜[1] 林贤福[1] 

机构地区：[1]浙江大学化学系

出　　处：《浙江大学学报（理学版）》2004年第5期544-547,共4页Journal of Zhejiang University（Science Edition）

基　　金：浙江省科技厅国际合作重点资助项目 ( 2 0 0 4C2 40 0 9)

摘　　要：研究枯草杆菌蛋白酶催化环糊精与癸二酸二乙烯酯在 DMF有机溶剂中的区域选择性反应 ,产物结构经IR、1 H NMR、1 3C NMR、MS和 DSC分析证实为单 - (2 - O-乙烯癸二酰 ) - β-环糊精 ;同时考察了三种不同的酶对反应的催化作用 .结果表明枯草杆菌蛋白酶和 Candida cylindracea脂肪酶对 β-环糊精在 C- 2位仲羟基的酯交换反应显示很高的选择性 ,而 lipozyme固定化酶在此体系中没有催化活性 .Transesterification of cyclomaltoheptaose (β-CD) with divinylsebacate was catalyzed by the alkaline protease from Bacillus subtilis in anhydrous DMF for 5 days forming the corresponding vinyl-β-CD derivative. The product was characterized with ESI-MS, ()~1H NMR, ()^(13)C NMR, IR and DSC. The results indicated that the product to be monosubstituted ester, with monoacylation occurring at the C-2 secondary hydroxyl groups of β-CD. The selectivity of CCL and lipozyme were also studied. The result indicated that CCL shows the same selectivity as alkaline protease from Bacillus subtilis, but lipozyme has no catalytic activity under the same reaction condition.

关 键 词：β-环糊精(β-CD) 区域选择性 仲羟基酰化 酶促合成 

分 类 号：O621.3[理学—有机化学]