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Biochemical characterization of an alkaline metallopeptidase secreted by a Pseudomonas fluorescens isolated from soil by Urszula Jankiewicz; Urszula Szawłowska; Monika Sobańska is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The extracellular endopeptidase synthesized by soil bacterium __Pseudomonas fluorescens__ was purified to homogeneity in a four‐step procedure. The enzyme was purified 45‐fold, with a 20% recovery. The endopeptidase appeared to be a monomer with a molecular mass of approx. 50 kDa. The enzyme was active in the pH range of 7 to 10. The optimal activity was detected at pH 9.0 and at 42 °C. Enzyme activity was inhibited by EDTA, EGTA and 1,10 phenanthroline, typical metalloprotease inhibitors. Ca^2+^ activated the enzyme while Zn^2+^, Co^2+^, Cd^2+^(in high concentration) strongly inhibited it. The presence of calcium ions strongly stabilized the enzyme with regard to thermal resistance. The amino acid sequence of fragments of the enzymatic protein determined by MS analysis revealed a high similarity to the sequences of other alkaline metalloendopeptidases of bacteria belonging to the genus __Pseudomonas.__ (© 2010 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)

Who reads Biochemical characterization of an alkaline metallopeptidase secreted by a Pseudomonas fluorescens isolated from soil?

Author

Urszula Jankiewicz; Urszula Szawłowska; Monika Sobańska

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Akademie Verlag; Wiley (ISSN 0233-111X)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)