Unraveling the binding mechanism between soybean protein isolate and selected bioactive compounds
Copyright © 2024 Elsevier Ltd. All rights reserved..
The present study was aimed to investigate the interactions between soybean protein isolate (SPI) with resveratrol (RESV) and lutein (LUT). The binding forces, molecular interactions and functional properties were explored by multi-spectroscopic analysis, molecular docking and functional property indexes between SPI and RESV/LUT. The RESV/LUT quenched SPI chromophore residues with static mechanism and the endothermic reaction. The SPI- RESV/LUT complexes were formed through hydrogen bond, electrostatic and hydrophobic interactions. Molecular docking confirmed van-der-Waals force as one of the important forces. The interaction of RESV/LUT led to SPI's secondary structure alterations with a decrease in α-helix and random coil and an increase in β-sheet and β-turns. RESV/LUT developed foaming and emulsifying properties of SPI and showed a significant decrease of the surface hydrophobicity with RESV/LUT concentrations increase attributed to SPI's partial unfolding. Our study exposed molecular mechanisms and confirmations to understand the interactions in protein- RESV/LUT complexes for protein industrial base promotion.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:447 |
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| Enthalten in: |
Food chemistry - 447(2024) vom: 30. Apr., Seite 139031 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Harimana, Yves [VerfasserIn] |
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| Links: |
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| Themen: |
Functional properties |
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| Anmerkungen: |
Date Completed 10.04.2024 Date Revised 10.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.foodchem.2024.139031 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Copyright © 2024 Elsevier Ltd. All rights reserved. | ||
| 520 | |a The present study was aimed to investigate the interactions between soybean protein isolate (SPI) with resveratrol (RESV) and lutein (LUT). The binding forces, molecular interactions and functional properties were explored by multi-spectroscopic analysis, molecular docking and functional property indexes between SPI and RESV/LUT. The RESV/LUT quenched SPI chromophore residues with static mechanism and the endothermic reaction. The SPI- RESV/LUT complexes were formed through hydrogen bond, electrostatic and hydrophobic interactions. Molecular docking confirmed van-der-Waals force as one of the important forces. The interaction of RESV/LUT led to SPI's secondary structure alterations with a decrease in α-helix and random coil and an increase in β-sheet and β-turns. RESV/LUT developed foaming and emulsifying properties of SPI and showed a significant decrease of the surface hydrophobicity with RESV/LUT concentrations increase attributed to SPI's partial unfolding. Our study exposed molecular mechanisms and confirmations to understand the interactions in protein- RESV/LUT complexes for protein industrial base promotion | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Functional properties | |
| 650 | 4 | |a Lutein | |
| 650 | 4 | |a Molecular docking | |
| 650 | 4 | |a Molecular interactions | |
| 650 | 4 | |a Resveratrol | |
| 650 | 4 | |a SPI | |
| 650 | 7 | |a Soybean Proteins |2 NLM | |
| 700 | 1 | |a Muhoza, Bertrand |e verfasserin |4 aut | |
| 700 | 1 | |a Munyandamutsa, Philip |e verfasserin |4 aut | |
| 700 | 1 | |a Gankhuyag, Javzan |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Shuang |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Yang |e verfasserin |4 aut | |
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