TiFN, Nieuwe Kanaal 9A, 6709 PA Wageningen, The Netherlands.
Laboratory of Food Chemistry, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
J Agric Food Chem. 2023 Jul 26;71(29):11228-11238. doi: 10.1021/acs.jafc.3c01589. Epub 2023 Jul 11.
In isolates from different pea cultivars, the legumin-to-vicilin (L:V) ratio is known to vary from 66:33 to 10:90 (w/w). In this study, the effect of variations in the L:V ratio on the pea protein emulsifying properties (emulsion droplet size () vs protein concentration ()) at pH 7.0 was investigated using a purified pea legumin (PLF) and pea vicilin fraction (PVF). Despite a different Γ, the interfacial properties at the oil-water interface and the emulsifying properties were similar for PLF and PVF. Hence, the L:V ratio did not affect the pea protein emulsifying properties. Further, PLF and PVF were less efficient than whey protein isolate (WPI) in stabilizing the emulsion droplets against coalescence. This was explained by their larger radius and thus slower diffusion. For this reason, the difference in diffusion rate was added as a parameter to the surface coverage model. With this addition, the surface coverage model described the versus of the pea protein samples well.
在不同豌豆品种的分离物中,已知豆球蛋白与伴豆球蛋白(L:V)的比例从 66:33 到 10:90(w/w)不等。在这项研究中,使用纯化的豌豆豆球蛋白(PLF)和豌豆伴豆球蛋白(PVF)研究了 L:V 比值变化对豌豆蛋白乳化性质(乳化液滴大小()与蛋白浓度())在 pH 7.0 时的影响。尽管 Γ 不同,但在油-水界面处的界面性质和乳化性质对于 PLF 和 PVF 是相似的。因此,L:V 比值不影响豌豆蛋白的乳化性质。此外,PLF 和 PVF 比乳清蛋白分离物(WPI)在稳定乳液液滴防止聚结方面效率更低。这可以用它们较大的半径和较慢的扩散来解释。由于这个原因,将扩散率的差异添加到表面覆盖率模型中作为一个参数。通过这种添加,表面覆盖率模型很好地描述了豌豆蛋白样品的 与 之间的关系。