酪蛋白经碱性蛋白酶Alcalase水解后,加入乙醇提取出的酪蛋白非磷肽(CNPPs)对血管紧张素转化酶(ACE)的活性有很强的抑制作用。采用凝胶过滤色谱Sephadex G-15和反相高效液相色谱(RP—HPLC)对CNPPs进行分离纯化,通过高效液相色谱/电喷雾电离质谱联用分析和氨基酸组成分析鉴定出一种抑制ACE活性肽,其氨基酸序列为Ser-Trp,ACE半抑制浓度为92.8μmol/L。
Casein non—phosphopeptides(CNPPs)which showed significant inhibitory activity against the angiotensin converting enzyme(ACE)could be obtained from casein by enzymatic hydrolysis and extracting with ethanol.CNPPs was first isolated by size exclusion chromatography(SEC)Sephadex G-15,and was further purified by reversed-phase HPLC.The pure peptide with ACE inhibitory activity was obtained,the amino acid sequence of which was identified as Ser-Trp by LC/ESI-MS and amino acid composition analysis. And the inhibitory concentration 50%(IC50)was 92.8μmol/L.