Rhizopus oryzae is the most common causative agent of zygomycosis and has a world-wide distribution with a high prevalence in tropical and subtropical regions. Chitin deacetylase acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. In the present study, some characters of the amino acid sequence of Chitin deacetylase of R.oryzae were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 20 kinds of amino acid; the theoretical pI of Chitin deacetylase was 5.03 and the theoretical molecular weight of Chitin deacetylase was 49177.9 Da; total number of atoms was 6786; the extinction coefficient was 108665(280 nm).The N-terminal of the sequence considered was M (Met) and the estimated half-life was 30 hours. The instability index (II) was computed to be 32.67. Aliphatic index was 67.91. There were 20 glycosylation sites,a signal peptide and conserved domains. It was a hydrolase.