Abstract：
α-Amylase inhibitory activity plays an important role in reducing blood glucose. Food-derived α-amylase inhibitors have attracted significant attention due to their safety. This study obtained peptides displaying α-amylase inhibitory activity from pepsin hydrolysate of quinoa protein concentrates. Gel filtration chromatography revealed that the <1 kDa component exhibited significant α-amylase inhibitory capability, while the purified component was identified via mass spectrometry identification. Six peptides with α-amylase inhibitory activity were selected, wherein the inhibitory ability of the peptide MMFPH was 66.41 % higher than the others. Molecular docking indicated that the peptide MMFPH residues restricted the α-amylase activity by binding to the active α-amylase site. The molecular interaction experiments showed that the peptides and α-amylase were in a fast-binding and slow-dissociation mode, allowing the small peptides produced via quinoa protein digestion to bind more rapidly to α-amylase, thus preventing a rise in blood glucose in vivo.
摘要：
α-淀粉酶抑制活性在降低血糖中起重要作用。食品来源的α-淀粉酶抑制剂因其安全性而备受关注。这项研究从藜麦蛋白浓缩物的胃蛋白酶水解物中获得了显示α-淀粉酶抑制活性的肽。凝胶过滤层析显示<1kDa组分表现出显著的α-淀粉酶抑制能力,而纯化的成分通过质谱鉴定。筛选出6种具有α-淀粉酶抑制活性的多肽,其中肽MMFPH的抑制能力比其他肽高66.41%。分子对接表明肽MMFPH残基通过与活性α-淀粉酶位点结合来限制α-淀粉酶活性。分子相互作用实验表明,多肽与α-淀粉酶呈快结合慢解离模式,允许通过藜麦蛋白消化产生的小肽更快地与α-淀粉酶结合，从而防止体内血糖升高。
