Resolution of 2-bromo-o-tolyl-carboxylic acid by transesterification using lipases from Rhizomucor miehei and Pseudomonas cepacia |
| |
| Affiliation: | 1. Centre de Bioingénierie Gilbert Durand, Département de Génie Biochimique et Alimentaire, UMR CNRS 5504, UMR INRA 792, INSA, 135 Avenue de Rangueil, F-31077 Toulouse Cédex 4, France;2. Aventis Pharma, Process Development Biotechnology, 9, quai Jules Guesde, F-94400 Vitry sur Seine, France;1. Department of Polymer Chemistry and Technology, Kaunas University of Technology, Radvilėnų av. 19, LT-50254 Kaunas, Lithuania;2. Lviv Polytechnic National University, Stepan Bandera 12, 79013 Lviv, Ukraine;1. Key Laboratory for Asymmetric Synthesis and Chiral Technology of Sichuan Province, Chengdu Institute of Organic Chemistry, Chinese Academy of Sciences, Chengdu 610041, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Chongqing Key Laboratory of Environmental Materials and Remediation Technologies, Drug Discovery Center of Innovation, Chongqing University of Arts and Sciences, 319 Honghe Ave., Yongchuan, Chongqing 402160, China;1. Faculty of Chemistry, Moscow State University, Moscow 119991 Russia;2. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences Leninsky prospect 31, Moscow 199071 Russia;1. Institute of Organic Chemistry and Technology, Faculty of Chemical Technology, University of Pardubice, Studentská 573, 532 10 Pardubice, Czech Republic;2. Institute of Macromolecular Chemistry of Czech Academy of Sciences, v.v.i., Heyrovského nám. 2, 162 06 Prague, Czech Republic |
| |
| Abstract: | Several lipases were screened for their ability to catalyze the enantioselective transesterification of 2-bromo-o-tolyl acetic acid. Amongst the preparations tested, the lipases from Rhizomucor miehei and Pseudomonas cepacia were selected. The best enantioselectivity was obtained with Rhizomucor miehei lipase immobilized on polypropylene (E=11.3), which was more stereoselective than the free form. Hydrophobic solvents with log P higher than 2.5 were the most suitable giving the highest E-values. In addition, factors such as the water activity and the reaction temperature had little effect on the resolution of the racemic mixture. The selectivity of the enzymes with respect to the substrate was also only weakly affected by the structure of the leaving alcohol except in the case of the iso-propyl group, which causes high steric hindrance. Operating conditions under reduced pressure were defined to resolve the racemic mixture with immobilized Rhizomucor miehei lipase. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
