Thermal Characterization of Purified Glucose Oxidase from A Newly Isolated Aspergillus Niger UAF-1

نویسندگان

  • Muhammad Anjum Zia
  • Khalil-ur-Rahman
  • Muhammad K. Saeed
  • Fozia Andaleeb
  • Muhammad I. Rajoka
  • Munir A. Sheikh
  • Iftikhar A. Khan
  • Azeem I. Khan
چکیده

An intracellular glucose oxidase was isolated from the mycelium extract of a locally isolated strain of Aspergillus niger UAF-1. The enzyme was purified to a yield of 28.43% and specific activity of 135 U mg(-1) through ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The enzyme showed high affinity for D-glucose with a Km value of 2.56 mM. The enzyme exhibited optimum catalytic activity at pH 5.5. Temperature optimum for glucose oxidase, catalyzed D-glucose oxidation was 40 degrees C. The enzyme showed a high thermostability having a half-life 30 min, enthalpy of denaturation 99.66 kJ mol(-1) and free energy of denaturation 103.63 kJ mol(-1). These characteristics suggest the use of glucose oxidase from Aspergillus niger UAF-1 as an analytical reagent and in the design of biosensors for clinical, biochemical and diagnostic assays.

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Purification and Properties of the Glucose Oxidase from Aspergillus Niger.

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عنوان ژورنال:
  • Journal of Clinical Biochemistry and Nutrition

دوره 41  شماره 

صفحات  -

تاریخ انتشار 2007