Chitinase, a pathogenesis-related protein, from bean seeds was purified to homogeneity by ammonium sulphate precipitation and chitin affinity binding technique from common bean seeds. Chitinase showed a molecular mass of nearly 32,500KDa by SDS-PAGE the enzyme was purified to 2.47-fold with a specific activity of 1,93U/mg using ammonium sulphate precipitation and the purification increased to 5.61fold with a specific activity of 4.83 U/mg after chitin affinity binding technique. The optimum pH and Temperature of the purified enzyme activity were found to be 5.4 and 45°C respectively. The thermostability test of the enzyme showed its stability till 50°C. The purified enzyme was enhanced by Na⁺, k⁺, Ca²⁺, and Mg² salts and inhibited by Hg²⁺ and Pb²⁺ salts at different concentrations. The enzyme exhibited a strong inhibitory action against Fusarium oxysporum, Fusarium solani, Fusarium moniliform, Alternaria alterna, and Candida albicans. The enzyme may represent an important defense protein in bean seeds. The finding suggests the possible usage of the purified enzyme as an antifungal agent against some phytopathogenic fungi in the field and its gene can be cloned and expressed in other plants for the production of fungal resistance once. Besides, the anticandidal activity suggests its possible pharmaceutical applications.