The effect of increasing sodium chloride concentration (cNaCl, 0-0.4 M) on the formation and rheological and microstructural properties of field pea protein isolate (FPPI)/chitosan (Ch) complex coacervates was investigated. The maximum turbidity and zeta potential of FPPI/Ch mixtures consistently decreased with the increasing cNaCl. The tertiary conformation of FPPI was altered to facilitate the aggregation of FPPI/Ch complexes via hydrophobic interactions. Changes in thermodynamic parameters during the titration of FPPI with Ch confirmed the addition of NaCl could cause the inhibition of electrostatic complexation and the induction of non-Coulombic interactions. FPPI/Ch complex coacervates exhibited first enhanced and then weakened viscoelastic properties and an initially tightened and then a loosened microstructure as the cNaCl increased. In summary, appropriate cNaCl favors the formation of FPPI/Ch complex coacervates with improved functionalities via the coordination of promoted hydrophobic interactions and inhibited electrostatic attractions, facilitating the application of this protein ingredient in food development.