Background: The protein aggregation process that forms senile cataracts is related to the pathway for making amyloid structures. With age the increase in β-secretase activity increases. β- and γ-secretase are enzymes that catalyze Amyloid-β Precursor Protein (APP) into β-amyloid (Aβ) structure. So that the β-amyloid (Aβ) formed must be cleaved using an enzyme containing protease to break down the proteins contained in the enzyme papain (Carica papaya L.) and zingibain enzymes (Zingiber officinale). So the In silico test is needed to see the binding ability between the proteolytic effects of the papain enzyme and the zingibain enzyme on β-amyloid (Aβ) protein. Determining the proteolytic potential of the papain enzyme and Zingibain enzyme against β-amyloid (Aβ) protein. Methods: collecting data of papain, zingibain enzyme and protein from RSCB and NCBI predicting the proteolytic potential of papain and zingibain enzyme against β-amyloid (Aβ) with docking simulation by In Silico Study and data analysis was carried out. Results: The binding interaction model is 1 for the papain enzyme and 0 for the zingibain enzyme with the binding affinity value for the papain enzyme is -697.2 and for the zingibain enzyme is -873.5. Conclusion: The papain enzyme isolated from papaya latex (Carica papaya L.) and Zingibain found in ginger (Zingiber officinale) has the ability to form bonds with β-amyloid (Aβ) protein so it has the potential to be developed as a useful proteolytic as a preventive for senile cataracts.