期刊
FOOD CHEMISTRY
卷 347, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.129052
关键词
Binding behavior; beta-conglycinin; Glycinin; Hyperoside; Docking simulation
资金
- National Natural Science Foundation of China [21808020]
- Sichuan Science and Technology Program [2019YFN0172]
- Key Laboratory of Coarse Cereal Processing, Ministry of Agriculture and Rural Affairs [2018CC16]
- Beijing Engineering and Technology Research Centre of Food Additives, Beijing Technology & Business University (BTBU)
This study investigated the interaction mechanisms between Hyperoside and two main soy proteins, showing that Hyperoside is stably located in the hydrophobic pockets of beta-conglycinin and glycinin. The conformation and microenvironment of the proteins changed after binding to Hyperoside, with a good affinity observed at 4 degrees C. The results suggest the potential for constructing an embedding and delivery system to enhance the benefits of Hyperoside in high value-added food products.
Hyperoside (HYP) is an important natural product that is widely distributed in fruits and whole grasses of various plants. It is also used by consumers as a healthy ingredient. This work explored the interaction mechanisms between HYP and two main soy proteins, namely, beta-conglycinin (7S) and glycinin (11S), using computational simulation and multi-spectroscopic technology. In this study, the docking and dynamic simulation showed that HYP was stable in the hydrophobic pockets of the proteins. The conformation and microenvironment of 7S/11S also changed after binding to HYP. The binding of HYP to 7S/11S was a state quenching with a good affinity at 4 degrees C. This result was determined from the binding constant values of (1.995 +/- 0.170) x 10(7) M-1 and (2.951 +/- 0.109) x 10(7) M-1, respectively. The 7S/11S-HYP complex delineated here will provide a novel idea to construct an embedding and delivery system in improving the benefits of HYP for the development of high value-added food products.
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