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Biochemistry (Moscow)

, Volume 74, Issue 1, pp 97–101 | Cite as

Catalytic activity and stability of xanthine oxidase in aqueous-organic mixtures

  • M. R. RashidiEmail author
  • M. H. Soruraddin
  • F. Taherzadeh
  • A. Jouyban
Article

Abstract

In the present study, bovine milk xanthine oxidase activity in various aqueous-organic mixtures and the effects of pH, temperature, and lyophilization on the enzyme activity have been investigated. The enzyme was incubated with xan-thine as the substrate in Sorenson’s phosphate buffer (pH 7.0) containing 0.1 mM EDTA, and the activity was determined spectrophotometrically in the absence and presence of different fractions of nine water-miscible organic solvents at 27–50°C and at different pH values ranging from 6 to 9. The organic solvents reduced the enzyme activity to different extents. In spite of these inhibitory effects, the enzyme showed relatively good stability in the aqueous-organic mixtures compared with the aqueous medium. A significant increase in the activity of the lyophilized enzyme was observed in pure organic solvents.

Key words

xanthine oxidase aqueous-organic mixtures enzyme activity thermal stability lyophilization 

Abbreviations

DMF

dimethylformamide

THF

tetrahydrofuran

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Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • M. R. Rashidi
    • 1
    Email author
  • M. H. Soruraddin
    • 2
  • F. Taherzadeh
    • 2
  • A. Jouyban
    • 3
  1. 1.Biotechnology Research CenterTabriz University of Medical SciencesTabrizIran
  2. 2.Analytical Chemistry Department, School of ChemistryTabriz UniversityTabrizIran
  3. 3.Pharmaceutical Chemistry Department, School of PharmacyTabriz University of Medical SciencesTabrizIran

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