1. Insight into the interaction and binding mechanism of a natural nonnutritive sweetener mogroside V with soybean protein isolates based on multi-spectroscopic techniques and computational simulations.
- Author
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Wu Y, Zhang Y, He Q, Qin Y, and Nie J
- Subjects
- Globulins chemistry, Globulins metabolism, Protein Binding, Antigens, Plant chemistry, Antigens, Plant metabolism, Computer Simulation, Seed Storage Proteins chemistry, Seed Storage Proteins metabolism, Molecular Docking Simulation, Triterpenes, Soybean Proteins chemistry, Soybean Proteins metabolism, Sweetening Agents chemistry, Sweetening Agents metabolism
- Abstract
As a natural low-calorie sweetener, Mogroside V (Mog-V) has gradually become one of the alternatives to sucrose with superior health attributes. However, Mog-V will bring unpleasant aftertastes when exceeding a threshold concentration. To investigate the possibility of soy protein isolates (SPIs), namely β-conglycinin (7S), and glycinin (11S) as flavor-improving agents of Mog-V, the binding mechanism between Mog-V and SPIs was explored through multi-spectroscopy, particle size, zeta potential, and computational simulation. The results of the multi-spectroscopic experiments indicated that Mog-V enhanced the fluorescence of 7S/11S protein in a static mode. The binding affinity of 7S-Mog-V was greater compared with 11S-Mog-V. Particle size and zeta potential analysis revealed that the interaction could promote aggregation of 7S/11S protein with different stability. Furthermore, computational simulations further confirmed that Mog-V could interact with the 7S/11S protein in different ways. This research provides a theoretical foundation for the development and application of SPI to improve the flavor of Mog-V, opening a new avenue for further expanding the market demand for Mog-V., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
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