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Characterization of a novel chitinase from a moderately halophilic bacterium, Virgibacillus marismortui strain M3-23
Essghaier, B.; Hedi, A.; Bejji, M.; Jijakli, H.; Boudabous, A.; Sadfi-Zouaoui, N. (2012). Characterization of a novel chitinase from a moderately halophilic bacterium, Virgibacillus marismortui strain M3-23. Annals of Microbiology 62(2): 835-841. dx.doi.org/10.1007/s13213-011-0324-4
In: Annals of Microbiology. Springer: New York. ISSN 1590-4261, more

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Author keywords
    Chitinase; Halotolerant; Thermotolerant; Virgibacillus marismortui;Catalytic domain

Authors  Top 
  • Essghaier, B.
  • Hedi, A.
  • Bejji, M.
  • Jijakli, H.
  • Boudabous, A.
  • Sadfi-Zouaoui, N.

Abstract
    A new chitinase produced by the moderately halophilic bacterium Virgibacillus marismortui strain M3-23 was identified and characterized. Distinguishable characteristics of high activity and stability at different pH, temperatures and salinity of M3-23 chitinase are reported. Analysis of the catalytic domain sequence from the enzyme highlighted its relationship to glycosyl hydrolase family 18. Comparison of the deduced chitinase sequence from strain M3-23 to known chitinases from Bacillus species showed low similarity (82%), suggested its novelty. This is the first report of the characterization of chitinase from the species V. marismortui. The halo- and thermo-tolerant nature of the chitinolytic enzyme allows its potential use in agricultural and industrial applications.

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