Niu Qing, Liu Enhui, Huo Chenkun, Zhang Fei, He Ruiqi, Yang Jie, Zhao Zhongkai
College of Smart Agriculture (Research Institute), Xinjiang University, Urumqi 830017, China.
Xinjiang Key Laboratory of Biological Resources Genetic Engineering, Urumqi 830017, China.
Foods. 2025 May 7;14(9):1644. doi: 10.3390/foods14091644.
This study investigated the effects of transglutaminase (TGase) content (0%, 0.5%, 1%, 1.5%) and heat treatment (25 °C, 70 °C, 80 °C, 90 °C) on the structure and gel properties of camel casein protein. The results indicate that a TGase concentration of 0.5% combined with a heat treatment of 90 °C in SDS-PAGE facilitates the aggregation and crosslinking of protein molecules to form polymers, with the degree of crosslinking increasing alongside the TGase concentration. In FTIR, the treatment with TGase and heat resulted in a shift of the absorption peak of the amide I band, indicating a transition of the secondary structure from a loose to an ordered configuration. Additionally, surface hydrophobicity and heat enthalpy values were significantly increased, while the thermal transition temperature of casein gradually decreased. Following TGase binding and heat treatment, casein protein molecules formed a network structure characterized by small pore sizes and close crosslinking. Rheological analysis revealed that 0.5% TGase treatment significantly lowered the gel formation point of casein, promoted gelation, and effectively enhanced the mechanical properties and water-holding capacity of the casein gels. These findings provide theoretical reference for the development of camel protein modification and gel products.
本研究考察了转谷氨酰胺酶（TGase）含量（0%、0.5%、1%、1.5%）和热处理（25℃、70℃、80℃、90℃）对骆驼酪蛋白结构和凝胶特性的影响。结果表明，在SDS-PAGE中，0.5%的TGase浓度与90℃的热处理相结合，促进了蛋白质分子的聚集和交联以形成聚合物，交联程度随TGase浓度增加而提高。在傅里叶变换红外光谱（FTIR）中，TGase和热处理导致酰胺I带吸收峰发生位移，表明二级结构从松散构型转变为有序构型。此外，表面疏水性和热焓值显著增加，而酪蛋白的热转变温度逐渐降低。经TGase结合和热处理后，酪蛋白分子形成了孔径小且交联紧密的网络结构。流变学分析显示，0.5%的TGase处理显著降低了酪蛋白的凝胶形成点，促进了凝胶化，并有效增强了酪蛋白凝胶的力学性能和持水能力。这些研究结果为骆驼蛋白改性及凝胶产品的开发提供了理论参考。
