|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
Chitinase; Halotolerant; Thermotolerant; Virgibacillus marismortui;Catalytic domain
|Authors|| || Top |
- Essghaier, B.
- Hedi, A.
- Bejji, M.
- Jijakli, H.
- Boudabous, A.
- Sadfi-Zouaoui, N.
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.