In this study, the thermal gelation and digestion properties of hen egg white (hen EW) proteins with different salts were investigated. Results show that the addition of neutral salt - sodium chloride (NaCl) decreased the gel hardness/resilience, increased gel lightness, aggregated particle size and digestibility of hen EW proteins significantly. In contrast, alkaline salts – phosphate and carbonate addition increased the gel resilience and strain tolerance as well as reduced the aggregated particle size and gel lightness of hen EW proteins due to the increase of solution pH and negative charge. Correlation analysis shows that the digestibility of hen EW gels was affected by gel viscoelasticity, molecule forces and texture. In conclusion, thermal gelation properties of hen EW proteins could be modulated by salts with different pH/ionic strength, and thus affected the protein digestion and peptide released.