This study was carried out to understand the activity of ${alpha}$-chymotrypsin, a proteolytic enzyme, to a oligopeptide in the presence of various coloring food additives. 1. The melting point of synthetic oligopeptide, Asp-Arg-Val-Tyr-Ile-His-Pro-D-Ala, ((8-D-Ala) angiotensin Ⅱ) was 210∼$212^{circ}C$. Chemical formula and molecular weight were $C_{44}H_{67}N_{13}O_{12}{cdot}2CH_3COOH{cdot}H_2O$ and 970.08, respectively. 2.The amino acid rations by acid hydrolysis were Asp : 1.01, Arg : 1.03, Val : 1.00, Tyr :40.94, Ile : 1.00, His : 1.05, Pro : 1.04, D-Ala : 1.03. 3. ${alpha}$-Chymotrypsin cleaved the oligopeptide bond between tyrosine and isoleucine (Tyr-Ile). 4. The addition of food coloring additives as determined by paper chromatogram, did not influence the inhibitory activity of ${alpha}$-chymotrypsin on oligopeptide, (8-D-Ala) angiotensin II.