Purification and characterization of chitinase secreted by Pseudoalteromonas sp. DXK012 isolated from deepsea sediment

Yang Liu, Zhuhua Chan, Runying Zeng

Daxue road 178#, Third Institute of Oceanography, Xiamen, 361005, China. Tel./Fax: +86-592-2195323


1-2-e37-2015

With the chitin as the sole carbon source, a chitinase-producing strain DXK012 was isolated from the deepsea sediment of 4826 m depth. The strain DXK012 belonged to Pseudoalteromonas, showing the closest phylogenetic affinity to Pseudoalteromonas arabiensis k53(T) (99.8% sequence similarity) and the stain was deposited with the number of CCTCC AB 2013143T. Cells were Gram-negative, with the optimum growth at 37℃, pH 7.5 and with the presence of 3% (w/v) NaCl. The chitinase from Pseudoalteromonas sp. DXK012 was extracellular enzyme and purified to homogeneity by ultrafiltration, DEAE-cellulose and Sephadex G-100 column chromatography. Molecular weight of purified chitinase was estimated to be ~36 kDa by SDS-PAGE. The optimal temperature and pH for the chitinase activity was 40℃ and 7.5, respectively. It acted on the GlcNAc-GlcNAc bonds, probably the GlcN-GlcNAc or GlcN-GlcN bonds. Mg2+ had positive effect on the enzyme activity, other metals inhibited the enzyme activity. In addition, the enzyme activity was inhibited by DTT, β-Mercaptoethanol (β-Me) and EDTA. Oligosaccharides mainly between hexose and octose were produced when chitin was hydrolyzed by this chitinase. The enzyme could be potentially used in industrial applications because of its interesting characteristics. Journal of Nature and Science, 1(2):e37, 2015.




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