机构地区: 东北农业大学食品学院
出 处: 《营养学报》 2012年第3期274-277,281,共5页
摘 要: 目的研究蛋清蛋白肽体外血管紧张素转化酶(ACE)抑制活性以及耐胃肠道消化稳定性。方法采用超滤分离蛋清蛋白酶解产物;利用高效液相色谱法测定蛋白酶水解物及其超滤各组分的体外ACE抑制活性。氨基酸自动分析仪测定ACE抑制活性较高组分(EWPH-Ⅲ)的氨基酸组成。体外模拟胃肠道消化试验测定EWPH-Ⅲ的消化稳定性。RP-HPLC法分析消化产物的组成变化。结果蛋清蛋白水解物的ACE抑制活性随着分子量的降低而增强(P<0.05),分子量小于3ku组分(EWPH-Ⅲ)的ACE抑制效果最好,其IC50值为0.049 mg/ml。EWPH-Ⅲ中疏水性氨基酸和必需氨基酸总量分别为49.51%和50.26%。经过胃肠道消化作用后,EWPH-Ⅲ的ACE抑制活性有所降低,消化产物的RP-HPLC分析结果显示EWPH-Ⅲ中多肽组分发生了明显的变化,胰酶消化产物中疏水性较强的多肽组分含量有所减少。结论蛋清蛋白肽具有较强的ACE抑制活性并且具有很高的营养价值,其ACE抑制活性随着阶段性的胃肠道消化而发生改变。 Objective To investigate the angiotensin I-converting enzyme(ACE) inhibitory activity of egg white-derived peptides and the impact of simulated gastrointestinal digestion on their stability in vitro.Method The egg white protein hydrolysate(EWPH) was separated by ultrafiltration.The ACE inhibitory activity of EWPH was measured by HPLC.Amino acid compositions of the most active compounds(EWPH-III) were detected by the automatic amino acid analyzer.In vitro simulated gastrointestinal digestion was carried out to study the stability of EWPH-III and the changes of composition were analyzed by RP-HPLC.Results EWPH showed significant decrease(P〈0.05) in ACE inhibitory activity with an increase in molecular weight(MW) of fractions values.The fractions with MW3000u(EWPH-III) exhibited the highest ACE inhibitory activity with IC50 values of 0.049 mg/ml.The total hydrophobic amino acids and essential amino acid contents were 49.51% and 50.26% respectively.After the simulated gastrointestinal digestion,the ACE inhibitory activity of EWPH-III decreased and the hydrophobic components of EWPH-III almost disappeared.Conclusion Egg white-derived peptides possessed potent ACE inhibitory activity and high nutritional value.The ACE inhibitory activity could be changed after the gastrointestinal digestion in vitro.