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.
摘要：
作为一种天然的低热量甜味剂，罗汉果苷V(Mog-V)已逐渐成为具有优越健康属性的蔗糖替代品之一。然而,当超过阈值浓度时，Mog-V会带来令人不快的余味。为了研究大豆分离蛋白(SPIs)的可能性，即β-伴大豆球蛋白(7S)，和大豆球蛋白(11S)作为Mog-V的增味剂，通过多光谱探索了Mog-V与SPIs的结合机制，颗粒大小,zeta电位,和计算模拟。多光谱实验结果表明，Mog-V以静态模式增强了7S/11S蛋白的荧光。与11S-Mog-V相比，7S-Mog-V的结合亲和力更大。颗粒大小和zeta电位分析表明，相互作用可以促进7S/11S蛋白的聚集，具有不同的稳定性。此外，计算模拟进一步证实Mog-V可以以不同的方式与7S/11S蛋白相互作用。本研究为开发和应用SPI改善Mog-V风味提供了理论基础,为进一步扩大Mog-V的市场需求开辟了新途径
