Rhodococcus erythropolis NCIMB

Rhodococcus erythropolis NCIMB 11540 has been employed as biocatalyst for the conversion of (R)- or (.S )-cyanohydrins to the corresponding (R)- or (S)-a-hydroxycarboxylic acids with an optical purity of up to >99% enatiomeric excess (ee) [27-29] the chiral cyanohydrins can separately be produced using hydroxynitrile lyase from Hevea braziliensis or from Prunus anygdalis [30]. Using the combined NHase-amidase enzyme system of the Rhodococcus erythropolis NCIMB 11 540, the chiral cyanohydrins were first hydrolyzed to the... 

A prochiral bis(cyanomethyl) sulfoxide was converted into the corresponding mono-acid with enantiomeric excesses as high as 99% using a nitrilase-NHase biocatalyst. The whole-cell biocatalyst Rhodococcus erythropolis NCIMB 11540 and a series of commercially available nitrilases NIT-101 to NIT-107 were evaluated in this study. As outlined in Figure 8.18, the prochiral sulfoxide may be transformed into five different products (plus enantiomeric isoforms), of which, three are chiral (A, B, and C) and two achiral (D and E). Only products A, B, and E were observed with the biocatalysts employed in this investigation. Both enantiomerically enriched forms of both A and C could be obtained with one of the catalysts used. The best selectivities are as follows (S)-A 99% ee, (R)-A 33% ee, (S)-C 66% ee, and (R)-C 99% ee, using NIT-104, NIT-103, NIT-108, and NIT-107 respectively. Each of these catalysts produced more... 

Table 15.2 Rhodococcus erythropolis NCIMB 11540 whole cell biohydrolysis isolated products.

In 2003, Griengl s group reported the hydrolysis of cyanohydrins by treatment with bacterial cells of Rhodococcus erythropolis NCIMB 11540, which have a highly active nitrile hydratase/amidase enzyme system. In this manner, (R)-2-chloromandelic acid and (R)-2-hydroxy-4-phenylbutyric acid, two important pharmaceutical intermediates, could be prepared in high optical and chemical yield after short reaction times (3 and 1.5 h, respectively) (Scheme 3.43). 

R=CgH5CO- Hydrolysis of cyclic P-aminonitriles 94% ee (amide) >99% ee (amide) >99% ee (amide) Rhodococcus equi A4 [62] Rhodococcus erythropolis NCIMB 11540(62] Rhodococcus sp. R312 [62]... 

Marchand, P., Rosenfeld, E., Erable, B., Maugard, T., Lamare, S., and Goubet, I. (2008) Coupled oxidation-reduction of butanol-hexanal by resting Rhodococcus erythropolis NCIMB 13064 cells in liquid and gas phase. Enzyme Microb. Technol,... 

Rhodococcus erythropolis NCIMB 11540 Cyanohydrins 2-Hydroxy acids 2-Hydroxy amides Enantioretentive transformation of enantiopure cyanohydrins [89-91]... 

R. erythropolis A4, Rhodococcus sp. R312, and R. erythropolis NCIMB 11540 were used in the hydrolysis of five- and six-membered ahcyclic trans-aminonitriles (Figure 11.6), which are the precursors of cyclic p-amino acids. The enzymes discriminated between the trans- and cis-isomers, the transformation of the former proceeding slowly or stopping at the amide stage. Moreover, hydrolysis of the latter resulted in excellent enantiopurity of the trans-amino acids or amides [38]. 

Rhodococcus sp. R-312 R. erythropolis A4 " R. erythropolis NCIMB 11540 P-Amino nitriles p-Amino amides and carboxylic acids Chemoenzymatic synthesis of unnatural amino acids and oligopeptides [98]... 

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