Bioinformatics Analysis on chitinase in Beauveria bassiana

Beauveria bassiana is one of the entomopathogenic fungi and has been successfully applied to bio-control insect pest. B.bassiana mainly depends on cuticle degrading enzymes including proteases, chitinases and lipases to penetrate host's cuticle. In the present study, some characters of the amino acid sequence of B.bassiana chitinase were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 20 kinds of amino acid, molecular weight was 36736.9 Da, theoretical pl was 6.20 and total number of atoms was 5141. It was a hydrolyze and stable protein and contain a signal peptide. There were 7 glycosylation sites, 10 alpha-helix, 17 sheets and some irregular coiled peptides. It was glycosyl hydrolase, a member of family 18 type II chitinases hydrolyze chitin.