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Abstract
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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
Submitted: 2010 October, 05
Accepted: 2010 November, 22
Published: 2011 January, 15 |
Abstract:
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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.
Key words: Bacillus halodurans, enzyme, extremophile environments, microbial peptidases, proteins, ,
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Abstract
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Cite this Reference:
S. Dabonné, A.P. Ahi, J.T. Gonnety and L.P. Kouamé, . A Soluble Aggregated Thermophile Metalloaminopeptidase Produced by an Alcalophile Strain of Bacillus halodurans. Current Research Journal of Biological Sciences, (1): 25-30.
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ISSN (Online): 2041-0778
ISSN (Print): 2041-076X |
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