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A Soluble Aggregated Thermophile Metalloaminopeptidase Produced by an Alcalophile Strain of Bacillus halodurans
並列摘要
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 V al-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 65℃.
延伸閱讀
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