The entomopathogenic fungus Metarhizium anisopliae (Metsch.) Sorokin is a well-characterized, broad host-range arthropod pathogen employed in biological control of agricultural pests. Entomopathogenic fungi actively invade their hosts through the cuticle by mechanical pressure, via apressorium formation, and enzymatic degradation by synergistic action of hydrolases, where chitinases are among the enzymes to be considered critical for host invasion. The present work describes the purification and characterization of spore surface chitinases from the entomopathogenic and acaricide fungus M. anisopliae. Spores from M. anisopliae produced in rice as substrate were immersed and strongly shacked in Tris-HCl buffer 50mM pH 8.0 containing 0.25% Triton X-100 for 5 min. The resulting supernatant was filtrated and applied on a DEAE-Sepharose column. Elution of proteins was done with a NaCl linear gradient (0-1.0 M). The fractions with chitinolytic activity were pooled and applied onto a gel filtration column Superose 12. All chromatographic steps were in FPLC purification system. The fractions of each purification step were analyzed by zymmograms and activity assays using 4-methyllumbeliferylchitotetraose (4-MU₄) as substrate. Zymmograms from extracted spore surface proteins showed six bands of chitinolytic activity. The next stages of this work will be the conclusion of the purification and characterization of the spore surface chitinases from M. anisopliae Financial support: FAPERGS, CAPES, CNPq, UFRGS.