The search for enzymes with histamine-degrading activity is of great interest, since it has great potential in the way of solving the problem of high histamine levels in food. In this study, the gene of a novel histamine-degrading enzyme, i.e., glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactobacillus plantarum was cloned and successfully expressed in Escherichia coli DH5α, with the recombinant host determined as histamine-degrading active. The recombinant GAPDH was then purified to homogeneity by ammonium sulfate fraction and gel filtration. The optimum pH and temperature were 5.5 and 40 °C and it was strongly resistant to SO₂ and ethanol. Afterwards, the histamine degradative activity of partially purified GAPDH in actual wine environments (grape and cherry wines) was examined by incubating the enzymes in the middle, near the end and completion of malolactic fermentation, and histamine in the corresponding contaminated wines was decreased by 36.8–52.4%, 59.6–66.9% and 83.1–85.5%, respectively.

寻找具有组胺降解活性的酶具有重要意义，因为它在解决食品中组胺含量高的问题方面具有巨大潜力。在这项研究中，一种新的组胺降解酶基因，即来自植物乳杆菌的甘油醛-3-磷酸脱氢酶 (GAPDH)被克隆并在大肠杆菌DH5α 中成功表达，重组宿主被确定为具有组胺降解活性。然后通过硫酸铵级分和凝胶过滤将重组GAPDH纯化至均质。最适 pH 值和温度为 5.5 和 40 °C，对 SO ₂有很强的抵抗力和乙醇。之后，通过在苹果乳酸发酵的中间、接近尾声和完成时孵育酶，检测了部分纯化的 GAPDH 在实际葡萄酒环境（葡萄和樱桃酒）中的组胺降解活性，相应受污染葡萄酒中的组胺降低了 36.8分别为 –52.4%、59.6–66.9% 和 83.1–85.5%。