固定化根霉脂肪酶的性质及在手性酯拆分中的应用

IMMOBILIZED LIPASE OF RHIZOPUS SP. Bc0-09m01: CHARACTERIZATION AND APPLICATION IN KINETIC RESOLUTION OF CHIRAL ESTER

通过载体筛选及固定化过程优化 ,选用硅胶 2 5℃吸附 4h、1%戊二醛交联 1h的方法对根霉 (Rhizopussp.Bc0 0 9m0 1)脂肪酶进行了固定化 .对固定化酶的各种酶学性质进行的研究表明 ,酶的最适作用温度为 40～ 45℃ ,最适作用pH为 7.5 ,在 4～ 30℃范围中性偏酸 (pH 4.0～ 9.0 )环境中比较稳定 ,固定化酶的热稳定性及pH稳定性较游离酶有较大幅度的提高 .将固定化酶用于拆分环氧丙醇丁酸酯 ,在转化率达到 5 3%时得到的残留底物对映体过量值 (ees)可达 90 % .固定化酶批式反应连续运行 10批后酶活仍保持 80 % .图 7表 2参

An immobilization method used for lipase was developed. Using this method lipase of Rhizopus sp. Bc0 09m01 was immobilized by adsorption onto silica gel at 25℃ for 4 h and then crosslinked with 1% glutaraldehyde for 1 h. The studies on the characteristics of immobilized lipase showed that the optimal temperature was 40～45℃ and optimal pH 7.5. The immobilized lipase was very stable under temperetune ranging from 4℃ to 30℃, quite stable in the range of pH 4.0～9.0. The optical resolution of racemic glycidyl butyrate was efficiently achieved by the immobilized lipase. The optical purity of the finally recovered (R)-glycidyl butyrate ee s was about 90% ee while conversion rate was 53% and final recovery was 15%. The remaining lipase activity of immobilized lipase was about 80% after being reused for 10 cycles. Fig 7, Tab 2 , Ref 13