Preparation and Identification of α-Amylase Inhibitory Peptides from Mung Bean Protein

被引：0
|
作者：
Li Y. [1 ,2 ]
Wang Y. [1 ]
Huang J. [1 ]
Shi F. [1 ]
机构：
[1] National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi
[2] Jiangsu Provincial Engineering Research Center for Bioactive Product Processing, Wuxi
来源：
Shipin Kexue/Food Science | 2024年 / 45卷 / 01期
关键词：
enzymatic hydrolysis; identification; isolation; mung bean protein; α-amylase inhibitory peptides;
D O I：
10.7506/spkx1002-6630-20230314-141
中图分类号：
学科分类号：
摘要：
In this study, sequential hydrolysis with pepsin followed by trypsin was conducted on total protein and protein fractions from mung bean. The difference in α-amylase inhibitory activity among the resulting hydrolysates was compared and the underlying reason was analyzed in terms of degree of hydrolysis, amino acid composition and molecular mass. The results showed that the total protein hydrolysate had the highest α-amylase inhibitory activity (16.51%). Compared with its fractions, the total protein showed the highest content of hydrophobic amino acids (32.68%) and degree of hydrolysis (6.28%), and the molecular mass of its hydrolysate was the lowest (< 20 kDa). Therefore, the total protein was selected to prepare α-amylase inhibitory peptides. Finally, 17 peptides with potential α-amylase inhibitory activity were discovered by the isolation and identification of peptides from mung bean protein. This study suggests that mung bean protein is a better food source of α-amylase inhibitory peptides than its protein fractions, which can be used in blood glucose-lowering functional foods or drugs. © 2024 Chinese Chamber of Commerce. All rights reserved.
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页码：58 / 64
页数：6
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