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• W3047188953 endingPage "106177" @default.
• W3047188953 startingPage "106177" @default.
• W3047188953 abstract "Soymilk is a popular health beverage worldwide, but its nutritional value is limited by soybean trypsin inhibitors (STIs). The interaction of tea polyphenols (TPs) with soymilk protein in the complex system was investigated in this work. TPs interacted with soymilk protein via static quenching process and hydrophobic interaction, with binding constant (K a ) of 5.22 × 10 3 L mol −1 at 298 K. Synchronous fluorescence suggested that the binding site of TPs to soymilk protein was mainly at Trp residues compared with Tyr residues. FTIR analysis revealed that hydrogen bonds were also observed in TPs-soymilk system. CD spectroscopy suggested that the protein conformation became more stable with addition of TPs by reducing β-sheet and random coil, and increasing α-helix and β-turn. The trypsin and chymotrypsin inhibitory activities (TIA and CIA) were reduced at 0.6 mg/g TPs in cooked soymilk from 788.3 ± 10.4 U/mL and 918.7 ± 18.0 U/mL to 388.3 ± 35.5 U/mL and 633.3 ± 52.8 U/mL, respectively. • Tea polyphenols (TPs) decreased trypsin and chymotrypsin inhibitory activities. • The quenching mechanism of soymilk protein by TPs was static quenching process. • TPs binding site to soymilk protein was mainly at Trp rather than Tyr residues. • Hydrophobic interaction and hydrogen bonds caused stable protein conformation." @default.
• W3047188953 created "2020-08-10" @default.
• W3047188953 creator A5003519879 @default.
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• W3047188953 date "2021-02-01" @default.
• W3047188953 modified "2023-09-29" @default.
• W3047188953 title "Effect of interaction between tea polyphenols with soymilk protein on inactivation of soybean trypsin inhibitor" @default.
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• W3047188953 doi "https://doi.org/10.1016/j.foodhyd.2020.106177" @default.
• W3047188953 hasPublicationYear "2021" @default.
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