Action patterns of two serine carboxypeptidases, one from yeast (Y) and the other from wheat bran (W), on N-[3-(2-furyl) acryloyl]-(Fua-) dipeptideamide substrates were examined by HPLC and amino acid analysis. In the reaction of the wheat enzyme the substrates were hydrolyzed to Fua-amino acid and no sufficient amount of Fua-dipeptides were detected on HPLC in the product mixtures. Very few or no free amino acids were observed by amino ...