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Adsorption Property and Affinity Chromatography of Polystyrene Derivative Sorbent Towards Cow's Milk Xanthine Oxidase by Noureddine Belattar is a Engineering article available to read on EtoBox.

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On the basis of the biospecific molecular recognition between complementary chemical groups of xanthine oxidase (XO) and their ligands particularly sulphated glycoaminoglycans and heparin. Poly (styrene chlorosulfonyl) particles modified by sulfonate sodium groups was synthesized and its adsorption property towards cow's milk XO was established. The adsorption of XO onto this functional polymer was performed in batch at 4 °C and at pH 6.0 during 30 min. of incubation. The adsorbed XO content at the interface allows establishing the chemisorption isotherm curve. The affinity association estimated from this adsorption isotherm according to the Langmuir equation was found to be significantly high in the magnitude of 1.25 × 10 6 M -1 . Affinity chromatography on column using this functional polymer as a stationary phase confirms its high ability to adsorb XO at low ionic strength. In fact, the xanthine oxidase of the crude extract is strongly adsorbed onto the sorbent and is eluted at high ionic strength with out any significant loss of its biological activity. The purified enzyme possesses a protein flavin ratio (PFR) of 6.05 with a specific activity of 1.78 UI/mg. On the other hand,

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Author

Noureddine Belattar

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0928-4931)

Published

2009

Language

EN

Field

Engineering (Physical Sciences)