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An activity coefficient model for proteins
Author(s) -
Agena Sabine M.,
Bogle I. David L.,
Pessoa Fernando L. P.
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(19970705)55:1<65::aid-bit8>3.0.co;2-v
Subject(s) - uniquac , virial coefficient , activity coefficient , solubility , chemistry , salt (chemistry) , thermodynamics , ovalbumin , consistency (knowledge bases) , osmotic coefficient , chromatography , aqueous solution , mathematics , non random two liquid model , physics , biology , immunology , geometry , immune system
Modeling of the properties of biochemical components is gaining increasing interest due to its potential for further application within the area of biochemical process development. Generally protein solution properties such as protein solubility are expressed through component activity coefficients which are studied here. The original UNIQUAC model is chosen for the representation of protein activity coefficients and, to the best of our knowledge, this is the first time it has been directly applied to protein solutions. Ten different protein‐salt‐water systems with four different proteins, serum albumin, alphacymotrypsin, beta‐lactoglobulin and ovalbumin, are investigated. A root‐mean‐squared deviation of 0.54% is obtained for the model by comparing calculated protein activity coefficients and protein activity coefficients deduced from osmotic measurements through virial expansion. Model predictions are used to analyze the effect of salt concentrations, pH, salt types, and temperature on protein activity coefficients and also on protein solubility and demonstrate consistency with results from other references. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 65–71, 1997.