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Hydrophobic chromatography of β‐galactosidase
Author(s) -
Chang C.T.,
McCoy B. J.,
Carbonell R. G.
Publication year - 1980
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/bit.260220211
Subject(s) - chemistry , desorption , adsorption , ionic strength , chromatography , diffusion , equilibrium constant , dispersion (optics) , hysteresis , reaction rate constant , ionic bonding , analytical chemistry (journal) , thermodynamics , kinetics , organic chemistry , ion , aqueous solution , physics , quantum mechanics , optics
The hydrophobic interaction of β‐galactosidase with Sepharose 4B substituted with 3,3′‐diaminodipropylamine was studied in both batch and column experiments. The equilibrium and the binding rate constants were determined for different phosphate buffer concentrations. The equilibrium constants exhibit a hysteresis effect, i.e., desorption constants are less than adsorption constants, and the higher the ionic strength to start the desorption, the larger the effect. The rate data are not satisfactorily described by a simple reversible first‐order model. The column chromatographic data are semiquantitatively described by a local equilibrium theory without axial dispersion or intraparticle diffusion.