Wang Yongze, Mei Lehe
Department of Chemical Engineering and Biochemical Engineering, Zhejiang University, Hangzhou 310027, China.
J Biosci Bioeng. 2007 Apr;103(4):345-9. doi: 10.1263/jbb.103.345.
Lipase was lyophilized with cyclodextrins to prepare lipase formulation suitable for the efficient resolution of allethrolone in ionic liquids. The effects of the type and amount of cyclodextrin used on lipase preparation were evaluated, and the properties of lyophilized lipase such as thermostability and pH sensitivity were investigated and compared with those of native lipase. The results showed that lipase lyophilized with cyclodextrins can achieve a higher conversion rate than the native one, and that lipase lyophilized with inorganic salts cannot improve the conversion rate of the resolution reaction. The catalytic behavior of the lyophilized lipase was strongly dependent on cyclodextrin type and reaction media. The activity of the lyophilized lipase increased as the amount of added cyclodextrins increased. The activity of the lipase lyophilized with cyclodextrins was optimum at pH 7 and 40 degrees C, which was similar to that of the native one, but the half-life of the lyophilized lipase was low compared with that of the native one.
将脂肪酶与环糊精一起冻干,以制备适用于在离子液体中高效拆分烯丙菊醇的脂肪酶制剂。评估了所用环糊精的类型和用量对脂肪酶制备的影响,并研究了冻干脂肪酶的热稳定性和pH敏感性等性质,并与天然脂肪酶进行了比较。结果表明,用环糊精冻干的脂肪酶比天然脂肪酶能实现更高的转化率,而用无机盐冻干的脂肪酶不能提高拆分反应的转化率。冻干脂肪酶的催化行为强烈依赖于环糊精类型和反应介质。随着添加环糊精量的增加,冻干脂肪酶的活性增加。用环糊精冻干的脂肪酶在pH 7和40℃时活性最佳,这与天然脂肪酶相似,但冻干脂肪酶的半衰期比天然脂肪酶低。