Liu Rui, Yan Xuebing, Liu Ruixin, Wu Qifan, Gao Yuhong, Muhindo Esther Mwizerwa, Zhi Zijian, Wu Tao, Sui Wenjie, Zhang Min
State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology, Tianjin, China.
Food Structure and Function (FSF) Research Group, Department of Food Technology, Safety and Health, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
J Sci Food Agric. 2024 Jan 30;104(2):818-828. doi: 10.1002/jsfa.12971. Epub 2023 Sep 29.
Lima bean protein isolate (LPI) is an underutilized plant protein. Similar to other plant proteins, it may display poor emulsification properties. In order to improve its emulsifying properties, one effective approach is using protein and polysaccharide mixtures. This work investigated the structural and emulsifying properties of LPI as well as the development of an LPI/xanthan gum (XG)-stabilized oil-in-water emulsion.
The highest protein solubility (84.14%) of LPI was observed and the molecular weights (M ) of most LPI subunits were less than 35 kDa. The enhanced emulsifying activity index (15.97 m g ) of LPI might be associated with its relatively high protein solubility and more low-M subunits (M < 35 kDa). The effects of oil volume fraction (ϕ) on droplet size, microstructure, rheological behavior and stability of emulsions were investigated. As ϕ increased from 0.2 to 0.8, the emulsion was arranged from spherical and dispersed oil droplets to polyhedral packing of oil droplets adjacent to each other, while the LPI/XG mixtures changed from particles (in the uncrowded interfacial layer) to lamellae (in the crowded interfacial layer). When ϕ was 0.6, the emulsion was in a transitional state with the coexistence of particles and lamellar structures on the oil droplet surface. The LPI/XG-stabilized emulsions with ϕ values of 0.6-0.8 showed the highest stability during a 14-day storage period.
This study developed a promising plant-based protein resource, LPI, and demonstrates potential application of LPI/XG as an emulsifying stabilizer in foods. © 2023 Society of Chemical Industry.
利马豆分离蛋白（LPI）是一种未得到充分利用的植物蛋白。与其他植物蛋白类似，它可能表现出较差的乳化性能。为了改善其乳化性能，一种有效的方法是使用蛋白质和多糖混合物。本研究考察了LPI的结构和乳化性能，以及LPI/黄原胶（XG）稳定的水包油乳液的形成。
观察到LPI的最高蛋白溶解度（84.14%），且大多数LPI亚基的分子量（M）小于35 kDa。LPI增强的乳化活性指数（15.97 m²/g）可能与其相对较高的蛋白溶解度和更多低分子量亚基（M < 35 kDa）有关。研究了油相体积分数（ϕ）对乳液液滴大小、微观结构、流变行为和稳定性的影响。随着ϕ从0.2增加到0.8，乳液从球形且分散的油滴排列转变为彼此相邻的油滴多面体堆积，而LPI/XG混合物从颗粒（在不拥挤的界面层中）转变为薄片（在拥挤的界面层中）。当ϕ为0.6时，乳液处于过渡状态，油滴表面同时存在颗粒和层状结构。ϕ值为0.6 - 0.8的LPI/XG稳定乳液在14天储存期内表现出最高的稳定性。
本研究开发了一种有前景的植物蛋白资源LPI，并证明了LPI/XG作为食品乳化稳定剂的潜在应用。© 2023化学工业协会。
