醋蛋中ACE抑制肽的分离及其活性保护的研究

ACE抑制肽在体内稳定性的研究对于其功能活性的保护具有重要意义。采用凝胶色谱层析法对经酶解后的醋蛋液进行分离纯化,收集具有较高抑制活性的多肽组分。再将其与卵磷脂结合形成复合物,目的是利用卵磷脂的乳化性保护多肽活性。利用FT-IR、XRD对复合物的结合效果进行验证分析,结果发现卵磷脂与活性肽结合后,活性肽的ACE抑制活性在体外模拟前后相较于未经结合处理得到明显的升高。红外光谱研究发现复合物中活性肽与卵磷脂发生相互作用。通过XRD进一步验证并推断是活性多肽被卵磷脂吸收后以无定形或分子态的形式存在。因此,可认为经过卵磷脂复合的多肽可以很好保留ACE抑制活性且可以降低其被胃肠道酶降解的风险。

Isolation of ACE inhibitory peptide in vinegar-egg hydrolysates and its activity protection WU Di

The stability of ACE inhibitory peptide in vivo is significant to protection of its biological active.Vinegar-egg hydrolysates were isolated and purified with Superdex gel chromatography.The high inhibitory activity components were collected and then were emulsified with lecithin in order to protect the bioactivity of ACE inhibitory peptides.The peptide-lecithin complex was investigated using FT-IR and XRD.The results showed that the bioactivity of ACE inhibitory peptides was increased after the binding treatment.The FT-IR showed that the interaction was detected in the peptide-lecithin complex.Further verification of the interaction using XRD proposed that ACE inhibitory peptide was absorbed by lecithin and existed in the form of amorphous and molecular state.Thus,the peptide-lecithin complex plays a role in retaining the bioactivity of ACE inhibitory peptides and reducing its risk of gastrointestinal enzyme digestion.