Abstract
The phase behavior of two aqueous binary protein mixtures, lysozyme-chymotrypsin and lysozyme-ovalbumin, was determined in ammonium sulfate solutions. Protein concentrations were determined in both phases as a function of pH and ionic strength. For lysozyme-chymotrypsin mixtures, the observed phase behavior was similar to that for each individual protein; the presence of the second protein had little influence. The phase behavior of lysozyme-ovalbumin mixtures, however, was different from that of the respective single-protein systems. Lysozyme and ovalbumin are found together in egg whites; their association is both pH and ionic-strength dependent. The association of proteins is a key determinant of protein solubility in salt solutions.
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