期刊
FOOD HYDROCOLLOIDS
卷 111, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2020.106177
关键词
Soymilk; Tea polyphenols; Soybean trypsin inhibitor; Structural information; Interaction
资金
- National Natural Science Foundation of China [31671870]
- Science and Technology Program of Guangzhou [201807010102]
- Science and Technology Program of Guangdong [2016B020203001]
- 111 Project [B17018]
Tea polyphenols interact with soy milk protein through static quenching and hydrophobic interactions, with a main binding site at Trp residues. This interaction stabilizes the protein conformation and reduces trypsin and chymotrypsin inhibitory activities in cooked soy milk when tea polyphenols are added.
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 x 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 beta-sheet and random coil, and increasing a-helix and beta-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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据