微水相中改性Ultrastable-Y分子筛固定化脂肪酶拆分(R,S)-2-辛醇  

Enzymatic Resolution of (R,S)-2-Octanol by Ultrastable-Y Molecular Sieve Immobilized-lipase in Microaqueous Media

作　　者：戴大章[1] 夏黎明[1] 

机构地区：[1]浙江大学材料与化学工程学院生物工程研究所,杭州310027

出　　处：《高等学校化学学报》2007年第12期2307-2310,共4页Chemical Journal of Chinese Universities

基　　金：中国博士后科学基金(批准号:20060401045)资助

摘　　要：采用改性Ultrastable-Y分子筛固定化P.expansumPED-03脂肪酶(PEL),利用固定化PEL在微水相中对(R,S)-2-辛醇进行拆分.结果表明,改性Ultrastable-Y分子筛固定化PEL所催化的拆分反应的转化率(c)和对映体过量值(e.e.)以及对映体选择性(E)均得到大幅度提高.介质类型和体系含水量对酶促拆分反应有较大的影响.在以正己烷为溶剂,含水量为0.8%的体系中,于50℃反应24 h的转化率(c)可达到理论值的97.68%,对映体过量值(e.e.)可达到98.75%.改性Ultrastable-Y分子筛固定化PEL催化效率高、立体选择性强,且催化性能稳定,在(R,S)-2-辛醇的酶法拆分方面具有良好的应用前景.The resolution of （R,S）-2-octanol was performed in microaqueous media by P. expansum PED-03 lipase（PEL） immobilized onto Uhrastable-Y modified molecular sieve. It was found that conversion（c）, enantiomeric excess（e, e. ）, and enantioselectivity（E） of the reaction catalyzed by PEL immobilized onto Ultra- stable-Y modified molecular sieve were much higher, compared with free PEL and PEL immobilized by other carriers. Media type and water content played an important role in the resolution of （R, S）-2-octanol catalyzed by Uhrastable-Y modified molecular sieve immobilized-PEL, and the reaction conversion （c） reached 97.68% of the theoretical value and the enantiomeric excess（e, e. ） reached 98.75% in n-hexane with 0. 8% water at ＂memorial＂ pH = 9.5 and 50 ℃ for 24 h. The modified Uhrastable-Y molecular sieve immobilized-PEL was a good biocatalyst with a fine enantioselectivity and stability, presenting a good promise in the enzymatic resolution of（ R, S） -2-octanol.

关 键 词：微水相 改性Ultrastable-Y分子筛 固定化脂肪酶 拆分 (R S)-2-辛醇 

分 类 号：O623.736[理学—有机化学]