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A chitinase cDNA named CHT1 was cloned from the hard tick, Haemaphysalis longicornis, and the enzymatic properties of its recombinant proteins were characterized. The CHT1 cDNA encodes 930 amino-acid (aa) residues including a 22 aa putative signal peptide, with the calculated molecular mass of the putative mature protein 104 kDa. The E. coli-expressed rCHT1 exhibited weak chitinolytic activity against 4MU-(GlcNAc)3. The rCHT1 protein with higher activity was obtained using recombinant Autographa californica multiple nuclear polyhedrosis virus (AcMNPV), which expresses rCHT1 under polyhedrin promoter. These findings suggest that the rCHT1 expressed in baculovirus-mediated Sf 9 cells has a high activity than E. coli-expressed rCHT1.