The objective of this study was to evaluate relationship with aggregation, secondary structures and gel properties of pork myofibrillar protein with different sodium chloride (1%, 2% and 3%). When the sodium chloride increased from 1 to 3%, the active sulfhydryl, surface hydrophobicity, hardness and cooking yield of myofibrillar protein were increased significantly (p < 0.05), the particle size, total sulfhydryl and Zeta potential were decreased significantly (p < 0.05), these meant the aggregations of pork myofibrillar protein were decreased. The changes of proteins aggregation induced the strongest intensity band of Amide I shifted up from 1660 cm−1 to 1661 cm−1, meanwhile, the β-sheet structure content was increased significantly (p < 0.05) with the sodium chloride increased. From the above, the lower proteins aggregation and higher β-sheet structure content could improve the water holding capacity and texture of pork myofibrillar protein gel.