Beibei Zhu

Tianjin University of Traditional Chinese Medicine

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Taoran Li

Jiangsu Province Hospital

Hongwu Wang

Tianjin University of Traditional Chinese Medicine

Ruiyang Hou

Tianjin University of Traditional Chinese Medicine

Zifan Zhang

Beijing Technology and Business University

Yubo Zhang

Tianjin University of Traditional Chinese Medicine

Yating Zhang

Tsinghua University

Yating Zhang

Hainan University

Zheng Li

University of Michigan–Ann Arbor

Chengxiang Ye

Tianjin University of Traditional Chinese Medicine

Wenqi Zhao

Tianjin University of Traditional Chinese Medicine

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Tianjin University of Traditional Chinese Medicine

Peking University

Jiangnan University

Ministry of Agriculture and Rural Affairs

Zhejiang University

Capital Medical University

Anshun University

Chongqing University of Posts and Telecommunications

Hebei Medical University

Second Hospital of Hebei Medical University

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Study on the binding behavior and functional properties of soybean protein isolate and β-carotene

Frontiers in Nutrition (2022)

Yating Zhang Wenqi Zhao Zhuqing Xing Beibei Zhu Ruiyang Hou

This study focused on the non-covalent interaction between soybean protein isolate (SPI) and β-carotene (BC). The conformational changes of SPI with β-carotene in varying proportions (BC/SPI: 2%, 4%, 6%, 8%, and 10%) were investigated by multi-spectroscopy and molecular docking. Results showed that the quenching mode is static quenching and binding affinity increased with temperature. The stoichiometry was 1:1, indicating there was only one binding site in SPI. The binding was based on entropy and primarily driven by hydrophobic interactions and its binding constant was in the order of 104 L⋅mol-1. The addition of the β-carotene affected the secondary structure of SPI resulting in an increase in α-Helix and a decrease in random coil and β-turn content, indicating protein aggregated and hydrophobic interactions occurred. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) verified that no new larger molecular weight substance was formed and no covalent interaction existed. Molecular docking corroborated that electrostatic and hydrophobic interactions were both involved in the formation of complexes, where hydrophobic interaction was the dominant one. Moreover, β-carotene improved 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, foaming capacity, and emulsifying stability of SPI. These findings provide useful information about the interaction mechanism of SPI and β-carotene, which contributes to the further development and application of SPI products rich in β-carotene in the food industry.

Hydrophobic effect

Binding constant

Non-covalent interactions

10.3389/fnut.2022.984490

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Citations (2)

Effect of polysaccharides on conformational changes and functional properties of protein-polyphenol binary complexes: A comparative study

International Journal of Biological Macromolecules (2023)

Zifan Zhang Taoran Li Yubo Zhang Juan‐Juan Shao Chengxiang Ye

Hydrophobic effect

Amide

10.1016/j.ijbiomac.2023.126890

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Citations (22)

Changes on the conformational and functional properties of soybean protein isolate induced by quercetin

Frontiers in Nutrition (2022)

Yating Zhang Ruiyang Hou Beibei Zhu Guangwei Yin Jian Zhang

The conformational changes and functional properties of SPI induced by quercetin was investigated via fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy and molecular docking. A decrease in the fluorescence intensity and a blue shift in the maximum wavelength were observed due to the binding process with fluorescent residues. The analysis of Stern-Volmer equation showed that the fluorescence quenching induced by quercetin took the form of static quenching, and the binding stoichiometry between SPI and quercetin was 1:1. The values of ΔH and ΔS were both positive illustrating that hydrophobic interaction was the primary binding force between quercetin and SPI. Results of FTIR and CD indicated that the binding with quercetin changed the secondary structure of SPI, resulting in a partially unfolded and more flexible structure. SDS-PAGE confirmed there was no covalent interaction between the two constituents. Molecular docking demonstrated that there were stable configurations and high matching degrees in both 11S and 7S proteins with quercetin via hydrogen bonds and hydrophobic interactions. Meanwhile, modification by quercetin enhanced the foaming and emulsifying capacities of SPI. These findings might provide theory reference for elucidation the mechanism of polyphenols-proteins interaction and development of related food additive products in future.

Hydrophobic effect

Docking (animal)

10.3389/fnut.2022.966750

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Citations (15)

Enhancement of non-covalent interaction between soy protein isolate and quercetin by sodium alginate

Food Chemistry (2024)

Taoran Li Yubo Zhang Juan‐Juan Shao Ruiyang Hou Zifan Zhang

Hydrophobic effect

Docking (animal)

Random coil

Electrostatic interaction

10.1016/j.foodchem.2024.140422

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Citations (3)