I work in a investigation about hydrolysis of protein of a andean grain and is very important for continue with my work what method is more effective for the activation or maybe is possible not to do it?
I don't think you need to do anything to activate the enzyme, if you are using a commercial preparation. Including a reducing agent and EDTA to prevent cysteine oxidation should assist with stability.
From the Sigma website:
"Papain is soluble in water at 10 mg/mL. Immediately prior to use, the enzyme is typically diluted in buffer containing ~5 mM L-cysteine. Activation/stabilizing agents include EDTA, cysteine, and dimercaptopropanol.21
Although papain solutions have good temperature stability, the solution stability is pH dependent. Papain solutions are unstable under acidic conditions, i.e., at pH values below 2.8, there is a significant loss in activity. For the active enzyme in solution, the loss in activity is about 1-2% per day, probably as a result of autolysis and/or oxidation."