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Soy peptide aggregates formed during hydrolysis reduced protein extraction without decreasing their nutritional value

Abstract

Upon enzymatic hydrolysis, soy protein isolate showed a strong tendency to aggregate, presenting a significant loss of valuable proteins. This study mainly focused on the large insoluble aggregates formed during proteolysis, and the influence of heating was further explored for better understanding the mechanism involved. Results from SDS-PAGE and amino acids analysis clearly showed that the insoluble aggregates formed upon hydrolysis were aggregated peptides, mainly attributed to the hydrophobic interactions between peptides with hydrophobic amino acid (Val, Ala, Leu, Ile, Tyr, Phe, Pro) and sulfur-containing (Met and Cys) residues. Heating of the hydrolysates further enhanced peptide-protein interactions through hydrophobic forces and disulfide bonds, accelerating the aggregation, where fractions from basic subunits of glycinin were particularly involved. Furthermore, taken the fact that aggregates had high proportion of essential amino acids into consideration, in vitro digestion properties of the aggregates were also investigated. Interestingly, the relatively pepsin-resistant aggregates showed a high degradability toward pancreatin, releasing low molecular weight peptides processing higher proportion of antioxidative amino acids, which therefore had a better antioxidant activity. These results indicated a potential use of the insoluble peptide aggregates as protein supplement or active delivery for human consumption.

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Publication details

The article was received on 04 Jun 2017, accepted on 30 Sep 2017 and first published on 02 Oct 2017


Article type: Paper
DOI: 10.1039/C7FO00812K
Citation: Food Funct., 2017, Accepted Manuscript
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    Soy peptide aggregates formed during hydrolysis reduced protein extraction without decreasing their nutritional value

    Y. Zhang, F. Zhou, M. Zhao, Z. Ning, D. Sun-Waterhouse and B. Sun, Food Funct., 2017, Accepted Manuscript , DOI: 10.1039/C7FO00812K

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