Adsorption equilibrium of fructosyltransferase on a weak anion-exchange resin.
The adsorption equilibrium of a glycoprotein, fructosyltransferase from Aureobasidium pullulans, on an anion-exchange resin, Sepabeads FP-DA activated with 0.1M NaOH, was investigated. The adsorption isotherms were determined at 20 degrees C in a phosphate-citrate buffer with pH 6.0 using the static method. Sodium chloride was used to adjust the ionic strength in the range from 0.0215 to 0.1215 mol dm(-3) which provided conditions varying from a weak effect of salt concentration on protein binding to its strong suppression. The equilibrium data were very well fitted by means of the steric mass-action model when the ion-exchange capacity of 290 mmol dm(-3) was obtained from independent frontal column experiments. The model fit provided the protein characteristic charge equal to 1.9, equilibrium constant 0.326, and steric factor 1.095 x 10(5).
Vanková
Katarína
K
Department of Chemical and Biochemical Engineering, Institute of Chemical and Environmental Engineering, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 81237 Bratislava, Slovakia.
Antosová
Monika
M
Polakovic
Milan
M
D000327:Adsorption; D000837:Anion Exchange Resins / Q000737:chemistry*; D002021:Buffers; D002852:Chromatography, Ion Exchange / Q000379:methods; D006602:Hexosyltransferases / Q000302:isolation & purification*; D007474:Ion Exchange; D008958:Models, Molecular; D015394:Molecular Structure; D012492:Salts / Q000737:chemistry; D013499:Surface Properties; D013816:Thermodynamics; D001426:Bacterial Proteins
D000837:Anion Exchange Resins; D002021:Buffers; D006602:Hexosyltransferases; D012492:Salts; C021451:inulosucrase; D001426:Bacterial Proteins