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本法以亚乙基阻断的对-硝基苯麦芽糖苷为底物，α-淀粉酶将其水解为乙基麦芽糖（Et-Gx）和对-硝基苯麦芽糖苷（Gy-pNP）；Gy-pNP进一步被α-葡萄糖苷酶水解，释放出对-硝基苯酚（p-NP）。该级联反应的终产物p-NP在405 nm处具有特征吸收峰，且其吸光度的变化速率与样本中α-淀粉酶的活性呈正比。通过动力学模式连续监测单位时间内OD₄₀₅的初始线性增幅（ΔOD₄₀₅/min），即可精准计算样品中α-淀粉酶的活力大小。
In this method, ethylidene-blocked p-nitrophenyl maltoside is used as the substrate. α-Amylase hydrolyzes it to ethylidene maltosaccharides (Et-Gx) and p-nitrophenyl maltosaccharides (Gy-pNP). Gy-pNP is further hydrolyzed by α-glucosidase to release p-nitrophenol (p-NP). The final product of this cascade reaction, p-NP, exhibits a characteristic absorbance peak at 405 nm, and its rate of absorbance increase is proportional to the α-amylase activity in the sample. By continuously monitoring the initial linear increase in OD₄₀₅ per unit time (ΔOD₄₀₅/min) in kinetic mode, the α-amylase activity in the sample can be precisely calculated.
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