Lavaei Yasaman, Varidi Mehdi, Nooshkam Majid
Department of Food Science and Technology, Faculty of Agriculture, Ferdowsi University of Mashhad (FUM), Mashhad, Iran.
Food Chem X. 2022 Aug 8;15:100408. doi: 10.1016/j.fochx.2022.100408. eCollection 2022 Oct 30.
Soy proteins are frequently used in the food industry; however, they have rigid and compact structure with relatively poor interfacial properties and solubility. This study was therefore aimed to modify techno-functional characteristics of soy protein isolate (SPI; 0.1% w/v) by conjugating to low acyl gellan gum (LAGG; 0.1, 0.2, and 0.3% w/v), through the Maillard reaction (at 90 °C for 90 min). The SPI-LAGG conjugates were confirmed by changes in pH, glycation degree (DG; up to 48%), Fourier transform infrared spectroscopy, and sodium dodecyl sulphate polyacrylamide electrophoresis. The conjugates were then classified into three clusters of low, medium, and high DG, -means clustering method. The low DG conjugate had lower surface hydrophobicity and foaming capacity, and higher thermal stability, solubility, emulsifying properties, foam stability, and antioxidant activity compared to the other clusters. This indicated that a low DG is required to enhance the functional properties of proteins.
大豆蛋白在食品工业中经常被使用；然而，它们具有刚性且紧密的结构，界面性质和溶解性相对较差。因此，本研究旨在通过美拉德反应（在90℃下反应90分钟），将大豆分离蛋白（SPI；0.1% w/v）与低酰基结冷胶（LAGG；0.1%、0.2%和0.3% w/v）共轭，以改善其技术功能特性。通过pH值变化、糖基化程度（DG；高达48%）、傅里叶变换红外光谱和十二烷基硫酸钠聚丙烯酰胺凝胶电泳对SPI-LAGG共轭物进行了确认。然后，采用K均值聚类法将共轭物分为低、中、高DG三个簇。与其他簇相比，低DG共轭物具有较低的表面疏水性和发泡能力，以及较高的热稳定性、溶解性、乳化性能、泡沫稳定性和抗氧化活性。这表明需要低DG来增强蛋白质的功能特性。
