A 912 bp full length cDNA encoding Teladorsagia circumcincta chitinase (TciCHT) was cloned and expressed in Escherichia coli. Recombinant TciCHT was purified and its enzyme assays performed. The predicted protein consisted of 304 amino acids and weighed about 34 kDa on sodium dodecyl (lauryl) sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The recombinant TciCHT was expressed as inclusion bodies and treated with 8M urea to denature the protein. Multiple alignments of the protein sequence of TciCHT with homologues from other helminths showed that the highest similarity (88%) to the CHT of Haemonchus sp, and 65-87% similarity to the other nematode CHT. Substrate binding sites and conserved regions were identified and shown to be conserved in other homologues. Enzyme assays were carried out using multiple substrates but failed to produce any activity. Recombinant TciCHT was recognised by antibodies in both serum and saliva from field-immune sheep in ELISA, however, that was not the case with nematode-naïve sheep. Given the importance of the enzyme and its recognition by the immune-sheep, Teladorsagia circumcincta chitinase might have potential as a vaccine candidate to control this common sheep parasite.