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Characterization and role of a metalloprotease induced by chitin in Serratia sp. KCK

  • Hyun-Soo Kim
  • Peter N. Golyshin
  • Kenneth N. Timmis
Original Paper

Abstract

A metalloprotease induced by chitin in a new chitinolytic bacterium Serratia sp. Strain KCK was purified and characterized. Compared with other Serratia enzymes, it exhibited a rather broad pH activity range (pH 5.0–8.0), and thermostability. The cognate ORF, mpr, was cloned and expressed. Its deduced amino acid sequence showed high similarity to those of bacterial zinc-binding metalloproteases and a well-conserved serralysin family motif. Pretreatment of chitin with the Mpr protein promoted chitin degradation by chitinase A, which suggests that Mpr participates in, and facilitates, chitin degradation by this microorganism.

Keywords

Metalloprotease Chitin Serratia Chitinase A 

Notes

Acknowledgments

We gratefully acknowledge MetaGenoMik Project of Federal Ministery for Science and Education (BMBF) and Fonds der Chemischen Industrie for generous support.

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Copyright information

© Society for Industrial Microbiology 2007

Authors and Affiliations

  • Hyun-Soo Kim
    • 1
  • Peter N. Golyshin
    • 1
    • 2
  • Kenneth N. Timmis
    • 1
    • 2
  1. 1.Department of Environmental MicrobiologyThe Helmholtz Center for Infection ResearchBraunschweigGermany
  2. 2.Institute for MicrobiologyTechnical University of BraunschweigBraunschweigGermany

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