Investigation on the amination to olefinic bond catalysed by Phenylalanine ammonialyase (PAL, EC 4.3.1.5) contained in Rhodotorula rubra (AS 2.166) whole cells, showed that only the two compounds, i.e. , 3-(2-furyl) acrylic acid (2i), 3-(3-methoxy-4-hydroxyphenyl) acrylic acid (2e), among the eight synthetic analogs of trans-Cinnamic acid: α-methyl-, β-methyl-, 4-nitro-, 4-methoxy-, 4-N, N-dimethylamino-, 4-methyl-Cinnamic acid and 2i, 2e, had been transformed into the corresponding optically pure L-isomer of α-amino acids, i.e., 3-(2- furyl) alanine (3i) and 3-(3-methoxy-4-hydroxyphenyl) alanine (3e). The chemical yields of 3i and 3e were 14.0% and 9.3% respectively, which are lower than that (44.8%) of L-Phenylalanine under the same conditions.

Key words: CINNAMYLIC ACID, RHODOTORULA, ENZYME CATALYSIS, PHENYLALANINE, ASYMMETRY