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

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Author(s): S. Dabonné | A.P. Ahi; J.T. Gonnety and L.P. Kouamé

Journal: Current Research Journal of Biological Sciences
ISSN 2041-076X

Volume: 3;
Issue: 1;
Start page: 25;
Date: 2011;
Original page

Keywords: Bacillus halodurans | enzyme | extremophile environments | microbial peptidases | proteins

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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