Journal of Pure and Applied MicrobiologyVol. 6 No. 1

Partial Purification and Characterization of Arthrobacter globiformis Protease

T.O. Femi-Ola┬╣* and O.O. Ojo

┬╣Department of Microbiology, ┬▓Department of Biochemistry, University of Ado- Ekiti, P.M.B. 5363, Ado- Ekiti, Nigeria.

Received on 26 June 2011 and accepted on 10 September 2011

 

ABSTRACT

An extracellular protease produced by Arthrobacter globiformis, an isolate from the gut of kola nut weevil Balanogastris kolae Desbr was partially purified and characterized in this study. The enzyme showed optimum activity at temperature of 60oC and pH 8.0. The molecular weight was estimated to be 35.7 kDa, while the Km and Vmax for the hydrolysis of casein were 71.43 mg/min/mL and 8.33mg/ mL respectively. The enzyme retained almost 80% of its relative activity after 20 minutes incubation at 60oC and its activity was not particularly influenced by majority of the cations tested. However, it was inhibited by Hg2+ and Fe3+.

Keywords : Protease, Arthrobacter, Casein, Cations, Weevil.