Protein salting-out: phase equilibria in two-protein systems |
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Authors: | Coen C J Prausnitz J M Blanch H W |
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Affiliation: | Department of Chemical Engineering, University of California, Berkeley, California 94720-9989. |
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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. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 567-574, 1997. |
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