Hassanvand Elham, Razavi Seyed Mohammad Ali
Center of Excellence in Native Natural Hydrocolloids of Iran, Ferdowsi University of Mashhad, PO Box: 91775-1163, Mashhad, Iran.
Center of Excellence in Native Natural Hydrocolloids of Iran, Ferdowsi University of Mashhad, PO Box: 91775-1163, Mashhad, Iran.
Int J Biol Macromol. 2024 Dec;282(Pt 5):137247. doi: 10.1016/j.ijbiomac.2024.137247. Epub 2024 Nov 3.
The small amplitude oscillatory shear (SAOS) rheological properties of complex coacervate of milk proteins with high (HMC), medium (MMC), and low (LMC) molecular weight chitosan in the optimal ratios of milk proteins to chitosan (15:1, 10:1, and 5:1, respectively) were measured. In addition, the morphological (SEM), structural (XRD), and thermal (DSC) properties of the complex coacervates were investigated in comparison with the milk protein concentrate. Complex coacervates showed the shear-thinning behavior due to a linear decrease of complex viscosity with increasing frequency. Furthermore, the highest complex modulus and the more compact structure under optimal conditions, in terms of the ratio of protein to chitosan and pH, revealed strong electrostatic bonding between proteins and chitosan. All coacervates showed a G' > G″ (Tanδ<1), indicating the formation of an interconnected gel-like structure that was described by the power law model. The maximum fracture stress was obtained at optimum conditions (R = 15:1, pH =6.7 for HMC; R = 10:1, pH =5.5 for MMC and R = 5:1, pH =4.6 for LMC), indicating the highest intermolecular interaction between milk proteins and chitosan. The coacervates had a completely amorphous structure similar to MPC, and according to DSC results, the ionic bonds between milk proteins and chitosan were not destroyed up to 300 °C. Coacervation leads to purified milk proteins at a low cost. In addition, the coacervates can be used for the encapsulation of heat-sensitive compounds, and also as a stabilizer to improve the texture of food.
测量了牛奶蛋白与高(HMC)、中(MMC)和低(LMC)分子量壳聚糖以最佳比例(牛奶蛋白与壳聚糖分别为15:1、10:1和5:1)形成的复合凝聚层的小振幅振荡剪切(SAOS)流变学性质。此外,与乳清蛋白浓缩物相比,研究了复合凝聚层的形态(扫描电子显微镜)、结构(X射线衍射)和热性质(差示扫描量热法)。复合凝聚层表现出剪切变稀行为,这是由于复合粘度随频率增加呈线性下降。此外,在最佳条件下,就蛋白质与壳聚糖的比例和pH值而言,最高的复合模量和更致密的结构表明蛋白质与壳聚糖之间存在强静电结合。所有凝聚层均表现出G' > G″(损耗因子<1),表明形成了由幂律模型描述的相互连接的凝胶状结构。在最佳条件下获得了最大断裂应力(HMC:R = 15:1,pH = 6.7;MMC:R = 10:1,pH = 5.5;LMC:R = 5:1,pH = 4.6),表明牛奶蛋白与壳聚糖之间的分子间相互作用最强。凝聚层具有与乳清蛋白浓缩物相似的完全无定形结构,根据差示扫描量热法结果,牛奶蛋白与壳聚糖之间的离子键在300°C之前不会被破坏。凝聚作用可以低成本得到纯化的牛奶蛋白。此外,凝聚层可用于包封热敏化合物,也可作为稳定剂来改善食品质地。