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    Abstract
2011 (Vol. 3, Issue: 1)
Article Information:

A Soluble Aggregated Thermophile Metalloaminopeptidase Produced by an Alcalophile Strain of Bacillus halodurans

S. Dabonné, A.P. Ahi, J.T. Gonnety and L.P. Kouamé
Corresponding Author:  Soumaila Dabonné 

Key words:  Bacillus halodurans, enzyme, extremophile environments, microbial peptidases, proteins, ,
Vol. 3 , (1): 25-30
Submitted Accepted Published
2010 October, 05 2010 November, 22 2011 January, 15
Abstract:

H4 strain isolated from Lake Bogoria was found to be Bacillus halodurans. The Bacteria produced an extracellular peptidase activity toward substrates Ile-pNA, Met-pNA and Val-pNA. It also hydrolyzed small peptides. A purification procedure including ion-exchange chromatography ion exchange DEAE and sizeexclusion chromatography followed by Sodium dodecyl sulphate-polyacrymalide gel electrophoresis (SDSPAGE) revealed the aggregated form of the enzyme. The three substrates are hydrolyzed by a single catalytic site. The enzyme inactivated by bestatin, and 1,10-phenanthroline is a metalloaminopeptidase whose activity is maximal at pH 9.0 and 65ºC.
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  Cite this Reference:
S. Dabonné, A.P. Ahi, J.T. Gonnety and L.P. Kouamé, 2011. A Soluble Aggregated Thermophile Metalloaminopeptidase Produced by an Alcalophile Strain of Bacillus halodurans.  Current Research Journal of Biological Sciences, 3(1): 25-30.
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ISSN (Online):  2041-0778
ISSN (Print):   2041-076X
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