The GH19 chitinase and hevein domains though connected by a lengthy loop, are restricted to be close by disulfide bridges. To our knowledge, this is the first report of any chitinase with intact hevein domain. During structure refinement, an extra domain could be traced and identified as hevein domain. ![]() Using X-ray diffraction data up to 1.66 Å, the structure was determined by Molecular Replacement using crystal structure of GH19 Chitinase-like protein from Hevea brasiliensis. Chitinolysis was also examined against insoluble chitin using SEM. The enzyme exhibited significant anti-fungal efficacy against phyto-pathogens such as Macrophomina phaseolina, Fusarium oxysporum and Sclerotium rolfsii. Peptide mass finger print analysis revealed the protein as an endo-chitinase which was further confirmed using chitin-agar assay. ![]() Chitinase from the leaves of Simarouba glauca, a plant used in traditional anti-inflammatory therapy is purified and characterized.
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