Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides from Aroase AP10 Hydrolysate of Octopus

The peptides from Aroase AP10 enzymatic hydrolysates of octopus proteins were isolated and tested for inhibitory activity against angiotensin converting enzyme (ACE). The Aroase AP10 hydrolysates were filtered through PM-10 membrane (M.W. cut-off 10,000) to obtain the peptides fractions with ACE inhibition activity. These fractions were applied to a Biogel P-2 column. Three active fractions (A, B, and C) were collected and applied to a SuperQ-Toyopearl 650S column chromatography, leading to the isolation of four active fractions (A-1, A-2, B-1, and C-1). Among the active fractions, C-1 had the highest ACE inhibitory activity ($IC_{50}=3.10{\mu}g$). The main composition of its amino acids is arginine, lysine, histidine and leucine, which cover about 60% of the total amino acids.

Aroase AP10에 의한 문어 가수분해물의 Angiotensin Converting Enzyme 저해 Peptide의 특성

문어육의 Aroase AP10 가수분해물을 제조하고 이들 가수분해물을 한외여과막을 통과시켜 회수한 분자량 10,000 Da이하의 저분자물질을 Bio-gel P-2 gel chromatography를 행하여 ACE 저해효과를 가지는 3개 획분을 분취하였다. 또한 이들 획분을 SuperQ-Toyopearl 650S column을 이용한 이온교환크로마토그래피에 의해 4개의 활성획분을 분리하였다. 이중 ACE 저해효과가 가장 높은 C-1 획분의 아미노산 조성은 arginine, lysine, histidine 및 leucine의 함량이 가장 많아 전체의 약 60%를 차지하였으며 $IC_{50}$은 $3.10{\mu}g$으로 나타났다.