Characterization of the structure, antioxidant activity and hypoglycemic activity of soy (Glycine max L.) protein hydrolysates

被引：40

作者：

Xu, Yue ^{[1
]}

Yang, Yang ^{[1
]}

Ma, Chun-min ^{[1
]}

Bian, Xin ^{[1
]}

Liu, Xiao-fei ^{[1
]}

Wang, Yan ^{[1
]}

Chen, Feng-lian ^{[1
]}

Wang, Bing ^{[1
]}

Zhang, Guang ^{[1
]}

Zhang, Na ^{[1
,2
]}

机构：

[1] Harbin Univ Commerce, Coll Food Engn, Key Lab Food Sci & Engn Heilongjiang Prov, Harbin 150028, Heilongjiang, Peoples R China

[2] Harbin Univ Commerce, Coll Food Engn, 1 Xuehai St, Harbin 150028, Heilongjiang, Peoples R China

来源：

FOOD RESEARCH INTERNATIONAL | 2023年 / 173卷

关键词：

Soy protein hydrolysate; Hydrolyze; Structure; Antioxidant activity; Hypoglycemic activity; LIMITED ENZYMATIC-HYDROLYSIS; ALPHA-GLUCOSIDASE; EMULSIFYING PROPERTIES; INHIBITORY PEPTIDES; BIOACTIVE PEPTIDES; PURIFICATION; IDENTIFICATION; FRACTIONATION; AMYLASE;

D O I：

10.1016/j.foodres.2023.113473

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

This study aimed to hydrolyze soy isolate protein (SPI) using five enzymes (alcalase, pepsin, trypsin, papain, and bromelain) in order to obtain five enzymatic hydrolysates and to elucidate the effect of enzymes on structural and biological activities of the resulting hydrolysates. The antioxidant and hypoglycemic activities of the soy protein isolate hydrolysates (SPIEHs) were evaluated through in silico analysis, revealing that the alcalase hydrolysate exhibited the highest potential, followed by the papain and bromelain hydrolysates. Subsequently, the degree of hydrolysis (DH), molecular weight distribution (MWD), amino acid composition, structure, antioxidant activities, and hypoglycemic activity in vitro of SPIEHs were analyzed. After enzymatic treatment, the particle size, polymer dispersity index (PDI), zeta-potentials, beta-sheet content and alpha-helix content of SPIEHs was decreased, and the maximum emission wavelength of all SPIEHs exhibited red-shifted, which all suggesting the structure of SPIEHs was unfolded. More total amino acids (TAAs), aromatic amino acids (AAAs), and hydrophobic amino acids (HAAs) were found in alcalase hydrolysate. For 1,1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, metal ion chelating activity, alpha-glucosidase inhibitory activity and alpha-amylase inhibitory activity, alcalase hydrolysate had the lowest IC50; alcalase hydrolysate and papain hydrolysate had the lowest IC50 for hydroxyl radical scavenging activity. Physiological activity of SPIEHs was evaluated thoroughly by 5-Axe cobweb charts, and the results revealed that alcalase hydrolysate exhibited the greatest biological activities.

引用

页数：11

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