Resolution of methylarylmethanols via oxidation with Nocardia corallina

Screening of liver acetone powders in the resolution of 1-phenylethanols and 1-phenylpropanols derivatives

“…7,8 The configuration of 2a was determined by comparing the specific rotation values with data from the literature. 6 …”

“…2,3 Optically active sec-alcohols can be prepared by asymmetric reduction of the corresponding ketone, 4,5 and by resolution of the racemic sec-alcohols via enantioselective oxidation. [6][7][8] Asymmetric hydrogen transfer is based on alcohol dehydrogenases that require nicotinamide cofactors, which have the disadvantage of requiring cofactor recycling. 9 The resolution of racemic sec-alcohols via enantioselective hydrolysis of their corresponding esters can be carried out using hydrolases that include lipases from microbial origin 10 and esterases from animal origin, specifically from the liver.…”

Nitrile hydratase activity of Nocardia corallina B-276

“…In Japan acrylamide is produced by the hydrolysis of acrylonitrile using resting cells of Rhodococcus rhodochrous J1; 4, 5 and 2-arylpropionitriles have been enantioselectively hydrolyzed to the corresponding amides or carboxylic acids using the bacteria of the genera Rhodococcus, [6][7][8][9] Agrobacterium, 9,10 and Pseudomonas. 11 Microorganisms of the genera Rhodococcus are some of the most common sources of NHases and amidases 12 and, due to the fact that some authors have taxonomically classified Nocardia corallina B-276 (bacteria which we have used previously in reactions of oxidation [13][14][15][16] ) as Rhodococcus corallinus, 17 we decided to study the possibility that Nocardia corallina B-276 could be used as a biocatalyst to hydrolyze nitriles.…”

On the organic solvent and thermostability of the biocatalytic redox system of Rhodococcus ruber DSM 44541

“…Biocatalytic oxidation/reduction of alcohols/ketones employing alcohol dehydrogenases has not yet become a general tool for preparative organic transformations, in particular on an industrial scale, due to several drawbacks, i.e., (1) the requirement for cofactor-recycling (Devaux-Basseguy et al, 1997;Hummel, 1997), (2) the general sensitivity of alcohol dehydrogenases towards elevated cosubstrateconcentrations, such as acetone (for oxidation) and 2-propanol (for reduction), (3) limited substrate concentration, and (4) cosubstrate-inhibition (Faber, 2000). As a consequence, these biochemical redox reactions usually show limited productivity due to the fermenting cells used that tolerate only limited cosubstrate concentrations (Fantin et al, 2000;Pérez et al, 1999;2001). Thus, for ketone reduction, 2-propanol was generally used in low concentrations (< 3% v/v) (Goswami et al, 2000;Nakamura et al, 1999); elevated concentrations of up to 15% v/v were reported by Heiss and Phillips (2000) and Schubert et al (2002).…”