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PARTIAL PURIFICATION AND SOME PROPERTIES OF PROTEASE FROM MICROSPORUM CANIS

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 جواد كاظم عبود الجنابي 6/11/2011 9:11:13 PM
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  PARTIAL PURIFICATION AND SOME PROPERTIES OF PROTEASE FROM MICROSPORUM CANIS Hayder Shkeir             Rabab Omran   Jawad K. Al-JenabiBiology Department/ College of Science/Babylon University Received 13/9/2005  Accepted 25/6/2006

ABSTRACT  Clinical strain Microsporum canis was isolated from specimen of patient with Tinea corporis in armand it has ability to produce extra cellular keratinolytic protease in a broth containing human hair. The enzyme was partial purified 35.8-fold from culture filtrate by sequential steps through salting out with ammonium sulfate precipitation (80% saturation), ion exchange Chromatography by batch wise ion exchange by CM- Cellulose cation resin and anion resin by DEAE-cellulose column.The partially purified enzyme had an optimum activity at pH 9 and maximum activity at pH11. The activity was stable in the alkaline pH 9 for 30 min at 25°C. Enzyme activity toward casein increased when temperature raised more than 20°C and maximal activity attained at 55° C. The enzyme was stable at temperature under 25?C and approximately 80% of its activity abolished by incubation of the enzyme at 60 °C for 30 min.  Protease had activation energy equal 3.314 Kcal/Mole that to be able to transform casein to product. On the other hand, the activation energy for denaturation was equal to 49.675 Kcal/Mole. The result of this experiment demonstrated that the enzyme is heat labile.Keywords: Microsporum canis, Protease, purification, properties


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