【摘要】 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)。更多还原

【Abstract】 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).更多还原