The complete cDNA (GenBank accession number DQ678929) and its corresponding gene (EF468349) of chitin deacetylase CDA2 from Mucor racemosus mycelium had been cloned by rapid amplification cDNA end (RACE) with specific degenerate primers. In contrast to previously obtained gene cda1, cda2 contained no intron sequence. It consisted of 1 378 bp nucleotides, comprising 23-bp 5’ untranslated region (UTR), 1 254bp open reading frame (ORF) and 101-bp 3’ UTR. The ORF encoded 418 amino acid (a.a.) residues including a 21 a.a. N-terminal signal peptide and a conserved polysaccharide deacetylase domain were located in an area of 150-272 a.a. residues. The results from subsequent construction of expressional vector pET28a-cda2 and prokaryotic expression revealed that molecular weight of recombinant protein CDA2 was about 46 ku and it was mainly found in inclusion bodies. The purified CDA2 showed chitin deacetylating activities. This work is necessary for further structural and functional exploration in chitin deacetylase CDA2 from M. racemosus.