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The complexation between lysozyme/carrageenan and ovalbumin/carrageenan was studied in situ using acidification. The complexes were analyzed in solutions with different NaCl concentrations and different protein/polysaccharide ratios. As the protein/polysaccharide ratio increased from 1:1 to 10:1, critical structure forming events (i.e., those associated with soluble, insoluble and large insoluble complexes) shifted to higher pH values for ovalbumin/carrageenan followed by decrease of G’ values at ratios of 5:1 and 10:1. The increase in the ratio of lysozyme/carrageenan complexes suppressed the critical pH transition points that led to the formation of large insoluble complexes from pH 12.0 until 1.0, and the values of G’ increased simultaneously, reaching the highest value at a ratio of 10:1. Addition of salt to the ovalbumin/carrageenan and lysozyme/carrageenan mixtures suppressed the electrostatic interaction …