The zeta potential of a molecule is an important property in the food industry, since the electrostatic potential of a material governs its ability to interact through ionic forces with other molecules in solution. In particular, emulsions that are kept in solutions with a high magnitude of the zeta potential are shown to be more stable over time, as the electrostatic repulsive forces of protein far from its isoelectric point can help prevent oil globule coalescence over time. However, modeling the zeta potential of protein is difficult given the anisotropy of protein molecules, the shifts in amino acid side chain ionization across pH, and understanding at what distance to measure the zeta potential from the molecular surface to accurately capture the shear plane between the particle and solvent under flow. In this work, we use the Poisson-Boltzmann Equation to model the net electrostatic surface potential of pea vicilin and legumin. We then use a weighted average of these globular proteins to predict the measured zeta potential in pea protein. The R² between the bioinformatically modeled net surface charge and the measured commercial isolate zeta potential is 0.987 between pH 2.50 and 9.50, and this equation predicted the zeta potential of a different commercial pea protein isolate with a standard error of 0.040. This shows that using the Poisson-Boltzmann Equation to solve for the net electrostatic surface potential, it is possible to accurately estimate the zeta potential of pea protein.

分子的 zeta 电位是食品工业中的一个重要特性，因为材料的静电电位决定了它通过离子力与溶液中其他分子相互作用的能力。特别是，保持在具有高 zeta 电位的溶液中的乳液随着时间的推移表现出更稳定，因为远离其等电点的蛋白质的静电排斥力可以帮助防止油球随着时间的推移聚结。然而，鉴于蛋白质分子的各向异性、氨基酸侧链电离随 pH 值的变化，以及了解从分子表面测量 zeta 电位以准确捕获分子表面之间的剪切平面的距离，模拟蛋白质的 zeta 电位是困难的。流动的颗粒和溶剂。在这项工作中，我们使用 Poisson-Boltzmann 方程来模拟豌豆 vicilin 和豆素的净静电表面电位。然后我们使用这些球状蛋白质的加权平均值来预测豌豆蛋白质中测得的 zeta 电位。R²的生物信息学建模的净表面电荷和所测量的商业分离物的ζ电势之间的pH为2.50和9.50之间0.987，并且该方程预测的一个不同的商业豌豆蛋白分离物的ζ电位与0.040标准误差。这表明使用泊松-玻尔兹曼方程求解净静电表面电位，可以准确估计豌豆蛋白的 zeta 电位。