Zhang Longteng, Li Qian, Zhang Wei, Bakalis Serafim, Luo Yongkang, Lametsch René
Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China; Department of Food Science, University of Copenhagen, 1958 Frederiksberg C, Denmark.
Department of Food Science, University of Copenhagen, 1958 Frederiksberg C, Denmark.
Food Chem. 2024 Feb 1;433:137315. doi: 10.1016/j.foodchem.2023.137315. Epub 2023 Sep 1.
This study aimed to illustrate the relationship among physicochemical properties, subunit composition and protein functionalities in a broad collection of commercial soy protein isolates (SPIs) from China and the EU. The results indicated that SPIs had large variations in glycinin/β-conglycinin composition, protein denaturation, and water- and oil-binding capacity (WBC and OBC) and solubility. These SPIs could be roughly divided into pre-denatured SPI, partially hydrolyzed SPI, and less modified SPI. The pre-denatured SPI with high surface hydrophobicity and large particle sizes showed reduced WBC and OBC due to increased protein aggregation, and partially hydrolyzed SPI showed high protein solubility owing to the exposure of hydrophilic regions and reduction in molecular size. The processing-induced physicochemical changes played a pivotal role in determining protein functionalities, whereas subunit composition affected protein functionality less. Overall, this study highlighted the obvious difference in raw material quality of commercial SPI, and provided promising methods for SPI categorization.
本研究旨在阐明来自中国和欧盟的大量商业大豆分离蛋白（SPI）的物理化学性质、亚基组成与蛋白质功能之间的关系。结果表明，SPI在大豆球蛋白/β-伴大豆球蛋白组成、蛋白质变性、水结合能力和油结合能力（WBC和OBC）以及溶解度方面存在很大差异。这些SPI大致可分为预变性SPI、部分水解SPI和低改性SPI。具有高表面疏水性和大粒径的预变性SPI由于蛋白质聚集增加而表现出降低的WBC和OBC，而部分水解SPI由于亲水区的暴露和分子尺寸的减小而表现出高蛋白溶解度。加工引起的物理化学变化在决定蛋白质功能方面起关键作用，而亚基组成对蛋白质功能的影响较小。总体而言，本研究突出了商业SPI原料质量的明显差异，并为SPI分类提供了有前景的方法。
