Infoscience

Conference paper

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)]

    Keywords: Resolution (of phenylalanine ; by enzymic transesterification) ; phenylalanine resoln enzymic transesterification

    Note:

    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)

    Reference

    • LGRC-CONF-1987-004

    Record created on 2006-04-18, modified on 2016-08-08

Fulltext

  • There is no available fulltext. Please contact the lab or the authors.

Related material