谷朊粉酶解物的制备及其ACE抑制肽的分离鉴定

以谷朊粉为原料，以血管紧张素转换酶（ACE）抑制率为指标，比较4种蛋白酶的酶解效果。采用超滤、葡聚糖凝胶色谱、反相高效液相色谱（RP-HPLC）的方法分离纯化ACE抑制肽并用电喷雾飞行时间质谱联用(ESI-TOF-MS)鉴定其结构。结果表明：碱性蛋白酶酶解3 h的谷朊粉酶解物具有较高的ACE抑制活性；超滤后，分子质量Mr<1 ku的组分具有较高的ACE抑制率；分离纯化后得到小肽的ACE抑制率高达（81.03±1.20）%；由ESI-TOF-MS质谱图得出该小肽的m/z为630.89，氨基酸序列为Trp-Phe-Gln-Pro（WFQP）。

Isolation and identification of ACE inhibitory peptide from wheat gluten hydrolysate

Using wheat gluten as raw materials and angiotensin-converting enzyme (ACE) inhibition rate as index, the effect of hydrolysis with four enzymes was compared. A novel ACE inhibitory peptide was purified by ultrafiltration, gel chromatography, RP-HPLC and then indentified by ESI-TOF-MS. The results showed that 3 h alkaline protease hydrolysates had higher ACE inhibitory activity; molecular weight of Mr less than 1 ku had higher ACE inhibition rate after ultrafiltration; the ACE inhibition rate of purified peptide from wheat gluten reached (81.03±1.31)%, the m/z was detected as 630.89 by ESI-TOF-MS, and the sequence and of purified peptide was Trp-Phe-Gln-Pro (WFQP).