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丙酮酸脱羧酶（pyruvate decarboxylase，PDC）主要存在于酵母中，是乙醇发酵的关键酶之一，催化丙酮酸脱羧生成乙醛。该产品可检测动物或植物组织、细胞或细菌、血清（浆）等样本中 PDC 的活性，其原理是 PDC 催化丙酮酸脱羧生成乙醛，添加乙醇脱氢酶（ADH）来进一步催化 NADH 还原乙醛生成乙醇和NAD⁺，NADH 在 340 nm有特征吸收峰，而NAD⁺没有，通过测定 340 nm 光吸收下降速率，来计算 PDC 活性。
Pyruvate decarboxylase (PDC) is primarily found in yeast and is one of the key enzymes in alcoholic fermentation, catalyzing the decarboxylation of pyruvate to produce acetaldehyde. This product is suitable for detecting PDC activity in samples such as animal or plant tissues, cells or bacteria, and serum (plasma). Its principle is that PDC catalyzes the decarboxylation of pyruvate to form acetaldehyde. Alcohol dehydrogenase (ADH) is added to further catalyze the reduction of acetaldehyde by NADH to generate ethanol and NAD⁺. NADH has a characteristic absorption peak at 340 nm, while NAD⁺ does not. PDC activity is calculated by measuring the rate of decrease in absorbance at 340 nm.
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