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Characterization of a chitinolytic enzyme from Serratia sp. KCK isolated from kimchi juice

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Abstract

The novel chitinolytic bacterium Serratia sp. KCK, which was isolated from kimchi juice, produced chitinase A. The gene coding for the chitinolytic enzyme was cloned on the basis of sequencing of internal peptides, homology search, and design of degenerated primers. The cloned open reading frame of chiA encodes for deduced polypeptide of 563 amino acid residues with a calculated molecular mass of 61 kDa and appears to correspond to a molecular mass of about 57 kDa, which excluded the signal sequence. The deduced amino acid sequence showed high similarity to those of bacterial chitinases classified as family 18 of glycosyl hydrolases. The chitinase A is an exochitinase and exhibits a greater pH range (5.0–10.0), thermostability with a temperature optimum of 40°C, and substrate range other than Serratia chitinases thus far described. These results suggested that Serratia sp. KCK chitinase A can be used for biotechnological applications with good potential.

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Acknowledgements

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

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Authors and Affiliations

  1. Department of Environmental Microbiology, The Helmholtz Center for Infection Research, Inhoffenstraße 1, 38124, Braunschweig, Germany

    Hyun-Soo Kim, Kenneth N. Timmis & Peter N. Golyshin

  2. Institute for Microbiology, Technical University of Braunschweig, Biozentrum, Braunschweig, Germany

    Kenneth N. Timmis & Peter N. Golyshin

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  1. Hyun-Soo Kim
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  2. Kenneth N. Timmis
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  3. Peter N. Golyshin
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Correspondence to Hyun-Soo Kim.

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Kim, HS., Timmis, K.N. & Golyshin, P.N. Characterization of a chitinolytic enzyme from Serratia sp. KCK isolated from kimchi juice. Appl Microbiol Biotechnol 75, 1275–1283 (2007). https://doi.org/10.1007/s00253-007-0947-3

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  • DOI: https://doi.org/10.1007/s00253-007-0947-3

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