School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, Jiangsu, China.
School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, Jiangsu, China.
Food Chem. 2024 Mar 15;436:137696. doi: 10.1016/j.foodchem.2023.137696. Epub 2023 Oct 15.
Bio-enzymes have shown broad application prospects in controlling mycotoxins due to their strong specificity, fast reaction rate and mild reaction conditions. However, the number of enzymes isolated, purified and characterized to degrade patulin (PAT) is limited. We expressed an aldo-keto reductase (MgAKR) from Meyerozyma guilliermondii in Escherichia coli. The results demonstrated that the purified MgAKR could convert PAT into ascladiol in vitro with NADPH serving as a coenzyme. Adding 300 μg/mL MgAKR resulted in an 88 % reduction of PAT in fresh pear juice without affecting its quality in the biodegradation process. The site-directed mutagenesis suggested that the interaction between MgAKR and PAT occurred through the active sites of Lys242 and Leu240. This study serves as a valuable theoretical reference for the development of enzymes aimed at detoxifying PAT in fruit and their derivatives.
生物酶由于其特异性强、反应速度快、反应条件温和，在控制霉菌毒素方面显示出广阔的应用前景。然而，能够降解棒曲霉素（PAT）的酶的分离、纯化和特性描述数量有限。我们在大肠杆菌中表达了来自 Meyerozyma guilliermondii 的醛酮还原酶（MgAKR）。结果表明，纯化的 MgAKR 可以在 NADPH 作为辅酶的情况下将 PAT 转化为 ascladiol。在生物降解过程中，添加 300μg/mL 的 MgAKR 可使新鲜梨汁中的 PAT 减少 88%，而不会影响其质量。定点突变表明，MgAKR 和 PAT 之间的相互作用发生在 Lys242 和 Leu240 的活性位点。这项研究为开发旨在解毒水果及其衍生物中 PAT 的酶提供了有价值的理论参考。
