<p>A new chitinase gene, cloned from the biocontrol <i>Chaetomium globosum</i> W7, was designated Cgchi18. Recombinant protein Cgchi18 with 535 amino acids was expressed in <i>Escherichia coli</i>, and purified by means of a column—free purification method relying on split intein, achieving a 12.39—fold purification and a 15.61% recovery yield. The maximum activity of this approximately 60-kDa protein was observed at 45&#xa0;°C and pH 5.0. Cgchi18 was activated by Mg²⁺ and Ba²⁺, but inhibited by Mn²⁺, Co²⁺, Cu²⁺, Zn²⁺, Ag⁺ and Hg²⁺. Cgchi18 showed high substrate specificity, only hydrolyzing β-1,4-glycoside bond in chitin and its derivatives, to liberate disaccharides or trisaccharides. For the degradation of colloidal chitin under optimal conditions, Vmax and Km of Cgchi18 were calculated as 8.05&#xa0;μmol/min/mg and 3.18&#xa0;mg/mL, respectively. Additionally, it exhibited antifungal activity and could have a degrading effect on the spread of hyphae of pathogenic fungi. In conclusion, the chitinase Cgchi18 identified from <i>C. globosum</i> has potential for industrial and agricultural applications.</p>