Abstract High pressure homogenization profoundly impacted the globular protein aggregation, and subsequently also its solubility and interfacial properties, using faba bean protein as model. The aggregate size and apparent molecular weight were studied by dynamic laser scattering and size exclusion chromatography before and after high pressure homogenization. High pressure homogenization dissociated large insoluble protein aggregates (>1 μm), leading to soluble supramolecular aggregates. Accordingly, 15 kpsi homogenization dramatically improved faba bean protein solubility (10 mg/ml) from 35 to 99% at neutral pH. High pressure homogenization resulted in certain level of protein unfolding with increased surface hydrophobicity. High pressure homogenized proteins adsorbed at the air-water interface faster than the untreated ones as a result of their higher surface hydrophobicity and the dissociation of insoluble protein aggregates. However, the supramolecular aggregates may compete with protein molecules at the interface, which then impaired the viscoelasticity of the interfacial network. This phenomenon observed may be related to the slower rate of rearrangement for supramolecular aggregates at interface due to a more complex structure. Consequently, the foaming capacity of 30 kpsi treated faba bean protein improved from 91 to 260% with 95% retention for 30 min. However, high pressure homogenization had negative effects on protein emulsifying property. This research revealed that plant globular protein aggregation status can determine both protein solubility and functionality. It has also provided insight how high pressure homogenization can be used strategically to modify protein functionality by modulating protein aggregation.

中文翻译：

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高压均质对蚕豆蛋白聚集与溶解度和界面性质的影响

摘要 以蚕豆蛋白为模型，高压均质对球状蛋白的聚集产生了深远的影响，进而影响了其溶解性和界面性质。在高压匀浆前后，通过动态激光散射和尺寸排阻色谱研究聚集体尺寸和表观分子量。高压匀浆解离大的不溶性蛋白质聚集体 (>1 μm)，导致可溶性超分子聚集体。因此，在中性 pH 下，15 kpsi 均质化显着提高了蚕豆蛋白溶解度 (10 mg/ml) 从 35% 到 99%。高压匀浆导致一定水平的蛋白质展开，表面疏水性增加。由于其较高的表面疏水性和不溶性蛋白质聚集体的解离，高压均质的蛋白质比未处理的蛋白质吸附在空气 - 水界面上的速度更快。然而，超分子聚集体可能会在界面上与蛋白质分子竞争，从而削弱界面网络的粘弹性。观察到的这种现象可能与由于更复杂的结构导致超分子聚集体在界面处的重排速度较慢有关。因此，30 kpsi 处理的蚕豆蛋白的发泡能力从 91% 提高到 260%，保留 95% 30 分钟。然而，高压均质对蛋白质乳化性能有负面影响。这项研究表明，植物球状蛋白质聚集状态可以决定蛋白质的溶解度和功能。它还提供了如何通过调节蛋白质聚集来战略性地使用高压均质来改变蛋白质功能的见解。