29302-73-6

Upstream product

• 644-36-0 o-methylphenylacetic acid 
• 85589-35-1 o-methylmandelic acid 
• 529-20-4 2-methylphenyl aldehyde 
• 85589-34-0 2-hydroxy-2-(2-methylphenyl)acetonitrile 

Downstream Products

• 129592-87-6 methyl 2-bromo-2-(2-methylphenyl)acetate 
• 404928-08-1 propyl (+/-)-2-bromo-o-tolyl-acetate 
• 404928-11-6 (+/-)-2-bromo-2-o-tolylacetic acid octyl ester 
• 37051-41-5 (+/-)-2-bromo-2-o-tolylacetic acid ethyl ester 
• 404928-10-5 (+/-)-2-bromo-2-o-tolylacetic acid benzyl ester 

Relevant academic research and scientific papers

Lipase-catalyzed enantioselective transesterification toward esters of 2-bromo-tolylacetic acids

Lipases from Candida antarctica, Pseudomonas cepacia and Rhizomucor miehei were tested in the resolution of seven racemic substrates belonging to the (RS)-2-bromo tolyl acetate ester category, but differing either in the position of the methyl substituent on the acyl part of the aromatic ring, or in the structure of the alkyl group. Lipase-catalyzed kinetic resolution via transesterification reaction between the ester and octanol in octane revealed that, of the three enzymes tested, P. cepacia lipase is the most efficient for resolution of the various racemates, with R-enantiopreference. In addition, the position of the methyl substituent was found to play a key role in governing the enantioselectivity of the reaction. Using P. cepacia lipase and 2-bromo-m/p-tolyl- or 2-bromophenylacetic acid esters E-values of 6.

Resolution of 2-bromo-o-tolyl-carboxylic acid by transesterification using lipases from Rhizomucor miehei and Pseudomonas cepacia

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.