燕麦麸蛋白ACE抑制肽的制备及性质研究

以燕麦麸为原料制备了燕麦麸蛋白,并利用蛋白酶对其酶解。测定了不同蛋白酶的水解产物的ACE抑制活性,以Alcalase和Trypsin酶解物活性最强。在此基础上进一步考察了Alcalase和Trypsin酶解物的DH对ACE抑制活性的影响,结果表明DH11.0%的Alcalase酶解物和DH12.2%的Trypsin酶解物有最大ACE抑制活性,分别达92.31%和86.36%。两种酶解物的肽组分相对分子质量均较低,大部分都低于1 000u。氨基酸分析表明ACE抑制肽中富含Glu、Leu、Pro和Phe。为了达到活性组分富集的目的,超滤技术是一种切实可行的方案。

Preparation and Characterization of Angiotensin Ⅰ- Converting Enzyme Inhibitory Peptides Derived from Oat Bran Protein

Oat bran protein was prepared from oat bran,and hydrolysed by several proteases for preparing angiotensin I-converting enzyme(ACE) inhibitory peptides.Results show that alcalase and trypsin are the suitable enzymes for producing peptides with strong ACE inhibitory activity.Furthermore,the relationship between degree of hydrolysis(DH) and ACE inhibitory activities of the hydrolysates was investigated.The alcalase hydrolysates with DH 11.0% and the trypsin hydrolysates with DH 12.2% exhibit the most potent activities(92.31% and 86.36%,respectively).The molecular weights of the two kinds of hydrolysates are mainly located below 1000 Da.The amino acid analysis indicates that the ACE inhibitory peptide is rich in Glu,Leu,Pro,and Phe.Moreover,ultrafiltration is an effective operation to obtain fractions with strong ACE inhibitory activities.