Zhang Yanna, Chen Xing, Li Xingwei, Tao Yuan, Zhang Nana, Yan Bowen, Zhang Hao, Fan Daming
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Food Res Int. 2025 Apr;206:116050. doi: 10.1016/j.foodres.2025.116050. Epub 2025 Feb 25.
Thermo-reversible gels (such as gelatin) have a wide range of applications in the food and pharmaceutical fields. This work reports a thermo-reversible gel prepared with pea protein isolate fractionated using ionic strength-shifting method (I: 0.5 → 0.125 M, I: 0.5 → 0.08 M, I: 0.5 → 0.06 M). The ionic strength-shifting fractioned pea protein isolate (ISS-PPI) can form thermo-reversible gels within a window of pH 4 and protein concentration of 8-12 %, all of which possessing high water holding capacities above 94.67 ± 2.33 %. The gel prepared from ISS-PPI of I had higher strength than the gels of I and I. Dynamic rheological measurement disclosed the thermo-reversibility of the gel being stable upon repeated heating and cooling process from 80 °C to 4 °C. The SDS-PAGE results showed that ISS-PPI were primarily composed of legumin, vicilin and convicilin and the latter two were considered mainly involved of reversible gelation. The internal pores of the I gel at 12 % protein concentration were consistently sized and most uniformly distributed, as observed by scanning electron microscopy (SEM). Hydrogen bonds were shown to be dominant in forming the gel network structure during the cooling process while hydrophobic interactions and disulfide bonds were not significantly involved. This research opened up thermal reversible gelation of pea protein which hosts great opportunities in plant-based jelly-like foods formulation.
热可逆凝胶（如明胶）在食品和制药领域有广泛应用。本研究报道了一种通过离子强度转换法（I：0.5 → 0.125 M，I：0.5 → 0.08 M，I：0.5 → 0.06 M）分级分离的豌豆分离蛋白制备的热可逆凝胶。离子强度转换分级分离的豌豆分离蛋白（ISS-PPI）在pH 4和蛋白质浓度为8-12%的范围内可形成热可逆凝胶，所有这些凝胶的持水能力均高于94.67 ± 2.33%。由I的ISS-PPI制备的凝胶比I和I的凝胶具有更高的强度。动态流变学测量表明，该凝胶在80°C至4°C的反复加热和冷却过程中热可逆性稳定。SDS-PAGE结果表明，ISS-PPI主要由豆球蛋白、豌豆球蛋白和伴豌豆球蛋白组成，后两者被认为主要参与可逆凝胶化。通过扫描电子显微镜（SEM）观察，蛋白质浓度为12%时I凝胶的内部孔隙大小一致且分布最均匀。结果表明，氢键在冷却过程中形成凝胶网络结构时起主导作用，而疏水相互作用和二硫键的参与不显著。本研究开启了豌豆蛋白的热可逆凝胶化，这在植物基果冻状食品配方中有很大机遇。
