Hashemi Hadi, Eskandari Mohammad Hadi, Khalesi Mohammadreza, Golmakani Mohammad-Taghi, Niakousari Mehrdad, Hosseini Seyed Mohammad Hashem
Department of Food Science and Technology, School of Agriculture, Shiraz University, Shiraz 71441-13131, Iran.
Department of Biological Sciences, University of Limerick, V94 T9PX Limerick, Ireland.
Foods. 2025 Jan 24;14(3):390. doi: 10.3390/foods14030390.
Protein conjugation with the Maillard reaction has received considerable attention in the past decades in terms of improving functional properties. This study evaluated the changes in the techno-functional properties of whey protein isolate (WPI), soy protein isolate (SPI), and albumin (Alb) after conjugation with basil seed gum (BSG). The conjugates were developed via the Maillard reaction. Various analyses including FT-IR, XRD, SEM, SDS-PAGE, DSC, RVA, rheology, zeta potential, emulsion, and foaming ability were used for evaluating conjugation products. Conjugation between proteins (WPI, SPI, Alb) and BSG was validated by FT-IR spectroscopy. XRD results revealed a decrease in the peak of BSG after conjugation with proteins. SDS-PAGE demonstrated the conjugation of WPI, SPI, and Alb with BSG. DSC results showed that conjugation with BSG reduced the of WPI, SPI, and Alb from 210.21, 207.21, and 210.90 °C to 190.30, 192.91, and 196.66 °C, respectively. The emulsion activity and emulsion stability of protein/BSG conjugates were increased significantly. The droplet size of emulsion samples ranged from 112.1 to 239.3 nm on day 3. Nanoemulsions stabilized by Alb/BSG conjugate had the smallest droplet sizes (112.1 and 143.3 nm after 3 and 17 days, respectively). The foaming capacity of WPI (78.57%), SPI (61.91%), and Alb (71.43%) in their mixtures with BSG increased to 107.14%, 85.71%, and 85.71%, respectively, after making conjugates with BSG. The foam stability of WPI (39.34%), SPI (61.57%), and Alb (53.37%) in their mixtures with BSG (non-conjugated condition) increased to 77.86%, 77.91%, and 72.32%, respectively, after formation of conjugates with BSG. Conjugation of BSG to proteins can improve the BSG applications as a multifunctional stabilizer in pharmaceutical and food industries.
在过去几十年中,蛋白质与美拉德反应的共轭作用在改善功能特性方面受到了广泛关注。本研究评估了乳清分离蛋白(WPI)、大豆分离蛋白(SPI)和白蛋白(Alb)与罗勒籽胶(BSG)共轭后其技术功能特性的变化。共轭物通过美拉德反应制备。采用包括傅里叶变换红外光谱(FT-IR)、X射线衍射(XRD)、扫描电子显微镜(SEM)、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)、差示扫描量热法(DSC)、快速粘度分析仪(RVA)、流变学、zeta电位、乳化和发泡能力等各种分析方法来评估共轭产物。通过FT-IR光谱验证了蛋白质(WPI、SPI、Alb)与BSG之间的共轭作用。XRD结果显示,与蛋白质共轭后BSG的峰值降低。SDS-PAGE证明了WPI、SPI和Alb与BSG的共轭作用。DSC结果表明,与BSG共轭后,WPI、SPI和Alb的熔点分别从210.21、207.21和210.90℃降至190.30、192.91和196.66℃。蛋白质/BSG共轭物的乳化活性和乳化稳定性显著提高。第3天乳液样品的液滴尺寸在112.1至239.3nm之间。由Alb/BSG共轭物稳定的纳米乳液液滴尺寸最小(3天和17天后分别为112.1和143.3nm)。与BSG共轭后,WPI(78.57%)、SPI(61.91%)和Alb(71.43%)与BSG混合物的发泡能力分别提高到107.14%、85.71%和85.71%。与BSG(非共轭条件)混合物中WPI(39.34%)、SPI(61.57%)和Alb(53.37%)的泡沫稳定性在与BSG形成共轭物后分别提高到77.86%、77.91%和72.32%。BSG与蛋白质的共轭作用可改善BSG在制药和食品工业中作为多功能稳定剂的应用。