Zhao Qiyue, Hu Xiaopei, Guo Kai, Li Suhong, Li Tuoping
College of Food Science, Shenyang Agricultural University, Shenyang 110866, China.
College of Food Science, Shenyang Agricultural University, Shenyang 110866, China.
Int J Biol Macromol. 2025 Feb;291:139154. doi: 10.1016/j.ijbiomac.2024.139154. Epub 2024 Dec 25.
The effects of TGase on hardness, water holding capacity (WHC), molecular forces, structural properties, microstructure and rheological behaviors of TGase-induced cowpea protein isolate gel (T-CPIG) and cowpea albumin gel (T-CPAG) were investigated. TGase significantly increased the hardness of gels and the most stable three-dimensional network structures were formed by adding 20 U/g and 28 U/g. Not only the non-network structure proteins of gels and free sulfhydryl groups were fewer but also the β-fold and β-angle relative contents were higher than cowpea protein isolate (CPI) and cowpea albumin (CPA). Hydrophobic interaction and the disulfide bond played main roles in the formation of T-CPIG and T-CPAG. Scanning electron microscopy and rheological properties of the gel suggested that the TGase addition significantly influenced the fundamental structure and mechanical properties of the T-CPIG and T-CPAG. Taken together, the findings shed light on the gelation mechanisms of TGase cowpea proteins.
研究了转谷氨酰胺酶（TGase）对TGase诱导的豇豆分离蛋白凝胶（T-CPIG）和豇豆白蛋白凝胶（T-CPAG）的硬度、持水能力（WHC）、分子间作用力、结构性质、微观结构及流变学行为的影响。TGase显著提高了凝胶的硬度，添加20 U/g和28 U/g时形成了最稳定的三维网络结构。凝胶的非网络结构蛋白和游离巯基不仅减少，而且β折叠和β转角的相对含量高于豇豆分离蛋白（CPI）和豇豆白蛋白（CPA）。疏水相互作用和二硫键在T-CPIG和T-CPAG的形成中起主要作用。凝胶的扫描电子显微镜和流变学性质表明，添加TGase显著影响了T-CPIG和T-CPAG的基本结构和力学性能。综上所述，这些发现揭示了TGase作用下豇豆蛋白的凝胶化机制。
