Abstract
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.
단백질 분해효소인 ${\alpha}$-chymotrypsin이 식품발색제의 존재하에 어떻게 oligopeptide에 작용하여 분해하는가를 알기 위하여 본 실험을 실시하였다. 1. Oligopeptide인 Asp-Arg-Val-Tyr-Ile-His-Pro-D-Ala(8-D-Ala${\cdot}$angiotensin II)의 융점은 210 ~ $212^{\circ}C$, 분자식은 $C_{44}H_{67}N_{13}O_{12}{\cdot}2CH_3COOH{\cdot}H_2O$, 분자량은 970.08이었다. 2. 산으로 가수분해 하였을 때 몰 비율은 Asp : 1.01, Arg : 1.03, Val : 1.00, Tyr :40.94, Ile : 1.00, His : 1.05, Pro : 1.04, D-Ala : 1.03이였다. 3. (8-D-Ala)angiotensin II의 oligopeptide에 ${\alpha}$-Chymotrypsin의 작용은 Tyr-Ile 결합에만 분해작용을 하였다. 4. 식품착색제의 첨가는 paper chromatogram 방법에 의해서 추정할때 oligopeptide, (8-D-Ala) angiotensin II에 대한 ${\alpha}$-Chymotrypsin의 저해작용에 아무런 영향을 끼치지 않았음을 볼 수 있다.
