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Protein salting‐out: Phase equilibria in two‐protein systems
Author(s) -
Coen C. J.,
Prausnitz J. M.,
Blanch H. W.
Publication year - 1997
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19970320)53:6<567::aid-bit4>3.0.co;2-k
Subject(s) - salting out , salting , chemistry , phase (matter) , chromatography , food science , organic chemistry , aqueous solution
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. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 567–574, 1997.