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This method uses ethyl blocked p-nitrophenyl maltotrioside as a substrate, which is hydrolyzed by α-amylase into ethyl maltose (Et-Gx) and p-nitrophenyl maltose (Gy-pNP). Gy-pNP can be further hydrolyzed by α-glucosidase into glucose and p-nitrophenyl (pNP)-glucoside. The final result of the amylase hydrolysis reaction and α-glucosidase action is the production of free p-nitrophenol (p-NP). p-NP has a characteristic absorption peak at 405nm, and its absorbance change is positively correlated with the activity of α-amylase in the sample.