Optical resolution of phenylalanine by enzymic transesterification

The acyl transfer of phenylalanine to MeOH by means of chymotrypsin starting from phenylalanine Pr ester has been studied. This transesterification turns out to be useful for producing optically pure phenylalanine esters as well as for the optical resoln. of phenylalanine. The L-phenylalanine Me ester may be obtained with yields >80%. The reaction medium required for transesterification represents a special case with respect to the use of org. solvents in enzymic catalysis, since MeOH can be regarded as a water miscible org. solvent, but behaves, in addn., as a cosubstrate. [on SciFinder (R)]

Published in:
Biocatalysis in Organic Media, 29, 375-80
CAN 108:183193 9-14 Biochemical Methods Inst. Genie Chim.,Ec. Polytech. Fed. Lausanne,Lausanne,Switz. Journal 0165-3253 written in English. 67-56-1 (Methanol) Role: RCT (Reactant), RACT (Reactant or reagent) (acylation of, chymotrypsin in); 9004-07-3 (Chymotrypsin) Role: ANST (Analytical study) (in phenylalanine resoln.); 2577-90-4P (L-Phenylalanine methyl ester) Role: PREP (Preparation) (prepn. of, by enzymic transesterification); 150-30-1 Role: PROC (Process) (resoln. of, by enzymic transesterification); 114260-57-0 (DL-Phenylalanine propyl ester) Role: RCT (Reactant), RACT (Reactant or reagent) (resoln. of, enzymic)

 Record created 2006-04-18, last modified 2018-03-17

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