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• W2625536645 abstract "Summary Isoflavone aglycone‐rich calcium‐binding soy protein hydrolysates were prepared by subcritical water treatment and subsequent protease hydrolysis. Contaminated β‐glucosidase in the Protease M preparation could effectively convert glycosides into aglycones. Compared with Alcalase hydrolysates, Protease M hydrolysates exhibited higher molecular weight (>5000 Da) and more hydrophobic characteristics because of its weaker proteolytic activity. The antioxidant activity of Protease M hydrolysates was obviously improved. Initial increased DPPH and ABTS radical scavenging rate of Protease M hydrolysates may be ascribed to the conversion of isoflavones (<30 min) and a gradual release of antioxidant peptides. In the later hydrolysis, a gradual exposure of isoflavones involved in the interior of heat‐induced protein aggregates was mainly responsible for further improved antioxidant activities. Higher calcium‐binding capacity (up to 7.86%) with lower yield of peptide–calcium complex was observed for Protease M hydrolysates. These results could help researchers to develop a feasible protocol for producing nutrient‐enhanced soy protein hydrolysates." @default.
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• W2625536645 date "2017-06-18" @default.
• W2625536645 modified "2023-10-11" @default.
• W2625536645 title "Preparation and characterisation of isoflavone aglycone-rich calcium-binding soy protein hydrolysates" @default.
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• W2625536645 doi "https://doi.org/10.1111/ijfs.13502" @default.
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