This study investigates investigated the mechanisms and variations in physicochemical properties and microstructures of potato protein gels at different pH levels under freezing conditions. Potato protein gels with a 15% protein concentration were prepared at pH 2, pH 7, and pH 10. The results showed that at pH 7, the gel exhibited roughness, pronounced granularity, a uniform pore size distribution, and a water-holding capacity of 97.12%. After freezing, the enthalpy was -228.13 J/g, leading to significant changes in moisture distribution and a reduction in water-holding capacity to 80.43%. At pH 10, increased hydrogen bonding (8.58%) and ionic bonding (2.03%) contributed to a denser, more ordered mesh structure with an enhanced water-holding capacity ( of 97.88%). The enthalpy was -227.85 J/g, which minimized moisture distribution changes and preserved a high water-holding capacity after freezing. In contrast, at pH 2, the gel exhibited a coarse and non-uniform structure, with a reduced water-holding capacity of 67.55%, increased enthalpy of -243.45 J/g, and elongated relaxation time. The freezing process led to ice crystal formation, which disrupted the protein network, particularly at lower pH levels. These findings offer a theoretical basis for optimizing potato protein gel structures and advancing the development of innovative potato-based products. • Effect of pH on the properties of potato protein gels. • Effect of freezing on the properties of potato protein gels. • Establishing a link between potato protein gels properties and structure after freezing, and to elucidate the mechanism of differences in potato protein gels properties during freezing.