Formation of ovalbumin-pectin coacervate complexes was analyzed in various NaCl concentrations and with various protein:polysaccharide ratios by isothermal titration calorimetry (ITC), by measuring zeta (ζ)-potentials, and by X-ray diffraction. The titration curve of a 1:1 ovalbumin:pectin coacervate complex formed in 0.01M NaCl displayed a region containing insoluble complexes, a region of considerable complex formation, and a region of complex dissociation. Changes in protein concentrations led to shifts in the region of insoluble complex formation (at the isoelectric point). At an ovalbumin:pectin ratio of 8:1, complex formation was suppressed. At NaCl concentrations of 0.05 and 0.1M, ovalbumin self-aggregation increased. When NaCl concentrations increased from 0.1 to 0.4M, complex dissociation was suppressed. X-ray diffraction of the ovalbumin-pectin coacervate complex showed a partially defined crystalline region from 27 to 20 suggesting that the structure of the complex is more organized than the individual amorphous polymers. Finally, this study addressed the effect of ovalbumin self-aggregates on ovalbumin-pectin complex formation.