The selected isolate of Microsporum canis JNU-FGC#503 was optimized for the production of proteases grows on casein containing basal salt medium. This exhibited the highest production on 6th day of incubation and optimum temperature for production was recorded at 45°C whereas pH was 10. During the studies on the activity of proteases with metal ions at the concentration of 50 mM/ml of reaction mixture, Cu2+, Mg2+ and Fe2+ ions enhanced the activity of enzyme whereas the concentration increased to 100 mM/ml, all the ions greatly inhibited the activity except Mg2+ and Fe2+. Stronger inhibitory effect was observed in the presence of Hg2+, Ag2+ and Zn2+. The effect of solvent on the enzyme activity at the rate of 50 mM/ml of reaction mixture, aniline and acetaldehyde enhance the activity of enzyme but acetic acid (5.05 U/ml) and formic acid (6.65 U/ml) showed maximum inhibition followed by ethanol (9.2U/ml). As the concentration was increased at the rate of 100 mM/ml, all solvents except aniline greatly decreased the activity. Among inhibitors, β- mercaptoethanol (6.15 U/ml) and EDTA (4.05 U/ml) were greatly inhibiting the activity whereas SDS and sodium meta bisulphate not affected the enzyme activity at this concentration. When the concentration was increased to 100 mM/ml of mixture, all the inhibitors greatly inhibited the activity except sodium meta bisulphate
