The enzymatic activity and partial characterization of proteases from fruits were evaluated and compared with proteases. The specific activity increased twofold after partial purification in both proteases. Partially purified proteases from showed good specific activity at pH 6.0-8.0 and residual activity of 70-100% for 60 min at 37-60 °C, similar to proteases. The value of proteases from was higher (253.32 µM) than that of proteases (234.94 µM). The use of specific protease inhibitors indicated the presence of cysteine and serine proteases. Proteases with molecular weight of 66.2-97 and 21-31 kDa were detected. proteases registered 73% hydrolysis using a soy protein concentrate, similar to the enzyme activity of proteases and commercial bromelain. These results demonstrate that proteases could be a potential alternative protease in the food industry.