Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
70896 | Journal of Molecular Catalysis B: Enzymatic | 2007 | 6 Pages |
Abstract
Lipase from Pseudomonas sp. (PSL) was immobilized on SBA-15 (a highly ordered hexagonal array mesoporous silica molecular sieve) through physical adsorption and the immobilized PSL was used in resolution of (R,S)-2-octanol with vinyl acetate as acyl donor. Enhanced activity and enantioselectivity were observed for the immobilized PSL compared with those of the free one. The effects of reaction conditions, such as solvents, temperature, water activity and substrate ratio were investigated. Under the optimum conditions, the residual (S)-2-octanol was recovered with 99% enantiomeric excess at 52% conversion. The results also indicated that the immobilized PSL maintained 90% of its initial activity even after reusing it five times.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Dahai Yu, Zhi Wang, Lifang Zhao, Yueming Cheng, Shugui Cao,