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Research Paper | March 1, 2013

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Partial purification and some properties of Vibrio haemolyticus protease

T. O. Femi-Ola, O. S. Bamidele

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Int. J. Biosci.3(3), 92-97, March 2013

DOI: http://dx.doi.org/10.12692/ijb/3.3.92-97

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Abstract

An extracellular protease of Vibro haemolyticus isolated from the gut of kolanut weevil Balanogastris kolae Desbr was partially purified and characterized in this study. The enzyme was purified in a two-step procedure involving ammonium sulphate precipitation and Sephadex G-150 gel filtration chromatography. The purified protease had an apparent molecular weight of 22.3kDa. The protease was found to have optimum activities at temperature of 50oC and pH of 8. The maximum velocity Vmax and Km of the protease produced during the hydrolysis of casein were 66.66mg/min/mL and 3.33mg/mL. The enzyme was almost 100% stable at 60oC even after 120 minutes of incubation. It was strongly activated by K+, while the enzyme activity was strongly inhibited by Fe3+ and Hg2+. .

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Partial purification and some properties of Vibrio haemolyticus protease

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