Adsorption equilibrium of fructosyltransferase on a weak anion-exchange resin

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• 作者：Katarí ; na Vaň ; ková ; Monika Anto&#x161 ; ová ; ; Milan Polakovič
• 关键词：Adsorption equilibrium ; Ion-exchange ; Protein ; Steric mass-action model ; Ionic strength ; Fructosyltransferase
• 刊名：Journal of Chromatography A
• 出版年：2007
• 期刊代码：47_00219673
• 类别：ch
• 出版时间：24 August 2007
• 卷：1162
• 期：1
• 页码：56-61
• 文件大小：159 K

摘要

The adsorption equilibrium of a glycoprotein, fructosyltransferase from Aureobasidium pullulans, on an anion-exchange resin, Sepabeads FP-DA activated with 0.1 M NaOH, was investigated. The adsorption isotherms were determined at 20 °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 × 10⁵.