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乙醛脱氢酶（EC 1.2.1.10，ALDH）是醛脱氢酶的一种，广泛存在于各种动物、植物和微生物体内。主要作用是将乙醛氧化成乙酸，在酒精代谢中起主要作用。在人类和许多动物体内，线粒体乙醛脱氢酶能把对生物体有害的醇类转化，所以在细胞解毒研究中乙醛脱氢酶受到高度关注，同时，乙醛脱氢酶在分子生物学以及相关疾病的检测方面有较广泛的研究应用。在辅酶Ⅰ存在的条件下，乙醛脱氢酶催化乙醛和 NAD+转化为乙酸和 NADH，在 340 nm 处的吸光值会增加，测定 340 nm 处的吸光值变化，可计算得出乙醛脱氢酶的活性。
Acetaldehyde dehydrogenase (EC 1.2.1.10, ALDH) is a kind of aldehyde dehydrogenase, which is widely present in various animals, plants and microorganisms. The main effect is the oxidation of acetaldehyde to acetic acid, which plays a major role in alcohol metabolism. In humans and many animals, mitochondrial aldehyde dehydrogenase (MDA) can convert alcohols that are harmful to organisms, so it has attracted great attention in the research of cellular detoxification. At the same time, aldehyde dehydrogenase has been widely used in molecular biology and the detection of related diseases. In the presence of coenzymeⅠ, acetaldehyde dehydrogenase catalyzes the conversion of acetaldehyde and NAD+ to acetate and NADH, and the absorbance value at 340 nm increases. The activity of acetaldehyde dehydrogenase can be calculated by measuring the absorbance value at 340 nm.
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