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从藜麦蛋白水解物中鉴定出一种新型的α-淀粉酶抑制活性肽。

Identification of a novel α-amylase inhibitory activity peptide from quinoa protein hydrolysate.

机构信息

National Soybean Processing Industry Technology Innovation Center, School of Food and Health, Beijing Technology and Business University, Beijing 100048, China.

National Soybean Processing Industry Technology Innovation Center, School of Food and Health, Beijing Technology and Business University, Beijing 100048, China.

出版信息

Food Chem. 2023 Mar 1;403:134434. doi: 10.1016/j.foodchem.2022.134434. Epub 2022 Sep 30.

DOI:10.1016/j.foodchem.2022.134434
PMID:36358076
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方面起着重要作用。由于其安全性,源于食物的α-淀粉酶抑制剂受到了广泛关注。本研究从藜麦蛋白浓缩物的胃蛋白酶水解物中获得了具有α-淀粉酶抑制活性的肽。凝胶过滤色谱显示,<1 kDa 组分表现出显著的α-淀粉酶抑制能力,而通过质谱鉴定鉴定了纯化的组分。选择了 6 种具有α-淀粉酶抑制活性的肽,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-淀粉酶的活性。分子相互作用实验表明,肽和α-淀粉酶处于快速结合和缓慢解离的模式,使通过藜麦蛋白消化产生的小肽能够更快地与α-淀粉酶结合,从而防止体内血糖升高。

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