산양유 Whey로부터 ACE 억제 Peptide의 분리 및 정제
Separation and Purification of Angiotensin Converting Enzyme Inhibitory Peptides derived from Goat's Milk Whey Hydrolysates
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본 연구는 산양유 whey에 다양한 가수분해 효소를 처리한 가수분해물에서 ACE 억제 능력을 가진 peptide를 분리하기 위해 실시하였다. Pepsin 가수분해물(72시간)에서 ACE 억제 능력이 가장 우수하였다(85.5%). Pepsin 가수분해물(72시간)을 gel filtration과 RP-HPLC에 의해 분리하여 ACE 억제 능력을 측정한 결과 ACE 능력이 가장 우수한 최종 분획(F- 4ed)에서 leucine(18.54%)이 가장 풍부하게 존재해 있었으며 아미노산 염기서열은 Leu- Lys-Asp-Tyr-Gly-Gly-Val-Ser-Leu과 Leu-Gly-Asp- Gly-Ala-Gly-Asp-Val-Ala-Phe의 염기서열인 것을 확인하였다. 따라서 본 실험의 결과 pepsin 처리한 산양유 whey 가수분해물에서 ACE 억제 능력이 우수하였으며, 향후 본 실험에서 분리된 ACE 저해 활성을 갖는 펩타이드를 대량 합성한 다음 in vivo test를 실시하여산업화 방안을 강구하여야 할 것으로 생각된다.
Abstract
ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat’s whey hydrolysates was 85.5% by pepsin for 72hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(18.54%) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-Gly- Val-Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. IC50 calibrated in peptic hydrolysates(72hrs), F-4, F-4e and F-4ed from goat’s whey hydrolysates by pepsin for 72hrs were 33.93, 28.75, 11.74 and 1.09mg/ml, respectively. From the results of this experiment, goat’s whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.
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