The chitin deacetylase gene was cloned from cDNA of Colletotrichum lindemuthianum ATCC 56676, and the open reading frame consisted of a possible prepro-sequence of 27 amino adds at the N-terminus and a mature: chitin deacetylase. The deduced amino acid sequence of the mature enzyme revealed 26% identity and 46% similarity with a chitin deacetylase from Mucor rouxii. The molecular mass of the protein estimated from the amino acid sequence data was 24.3 kDa, which was in good agreement with the MALDI-TOF MS analysis data of the purified protein (24.17-24.36 kDa). The gene product was overexpressed in Escherichia coli cells as a fusion protein with six histidine residues at its C-terminus. The fusion protein formed inclusion bodies, but chitin deacetylase activity was restored from the inclusion bodies by a simple renaturation step with 8 M urea treatment. The recombinant enzyme was purified by affinity chromatography and gel filtration steps, and had a final specific activity of 4.22 omits mg(-1) of protein. Trypsin digestion of the recombinant enzyme resulted in 2.1-fold increase in activity, suggesting that the removal of the prepro-domain from the recombinant enzyme resulted in an increase in its activity.