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来自海洋放线菌属菌株SCN 63 - 126的脱氧雪腐镰刀菌烯醇脱氢酶的特性及其应用

Characterization of deoxynivalenol dehydrogenase from Pelagibacterium sp. SCN 63-126 and its application.

作者信息

Xu Wei, Yao Jiayi, Ma Jingbo, Lu Chen, Wang Chenfei, Sun Yurong, Guang Cuie, Mu Wanmeng

机构信息

State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, P. R. China.

Department of Neurology, Affiliated Children's Hospital of Jiangnan University, Wuxi, Jiangsu, 214122, China.

出版信息

Arch Microbiol. 2024 Dec 5;207(1):9. doi: 10.1007/s00203-024-04208-9.

DOI:10.1007/s00203-024-04208-9
PMID:39636447
Abstract

Deoxynivalenol (DON), a type-B trichothecene mycotoxin, is primarily produced by Fusarium species and widely pollutes wheat and other grains. Enzymatic treatment of DON has been widely studied in recent years. Here, we present the biochemical identification of the DON dehydrogenase from Pelagibacterium sp. SCN 63-126 (Pe DDH). After removing the signal peptide, Pe DDH is effectively expressed in its soluble form. Biochemical identification indicates that the optimal temperature and pH of Pe DDH against DON is 35 ℃ and pH 8.5. Furthermore, Pe DDH is activated significantly in the presence of Ca, Mg, and Cu, and alternatively activated by pyrroloquinoline quinone (PQQ), phenazine methosulfate (PMS), and 2, 6-dichlorophenolindophenol (DCPIP). When PQQ, PMS, and DCPIP are combined, Pe DDH (60 µg/mL) effectively degrads DON (150 µM) in just 5 min, suggesting a synergistic effect of three cofactors on DON degradation. All these results suggest a great potential of Pe DDH in the control of DON contamination.

摘要

脱氧雪腐镰刀菌烯醇(DON)是一种B型单端孢霉烯族真菌毒素,主要由镰刀菌属产生,广泛污染小麦和其他谷物。近年来,对DON的酶促处理已得到广泛研究。在此,我们展示了来自远洋杆菌属菌株SCN 63-126(Pe DDH)的DON脱氢酶的生化鉴定。去除信号肽后,Pe DDH以可溶形式有效表达。生化鉴定表明,Pe DDH作用于DON的最佳温度和pH分别为35℃和pH 8.5。此外,Pe DDH在Ca、Mg和Cu存在时被显著激活,并且可被吡咯喹啉醌(PQQ)、硫酸吩嗪(PMS)和2,6-二氯酚靛酚(DCPIP)激活。当PQQ、PMS和DCPIP联合使用时,Pe DDH(60μg/mL)在短短5分钟内就能有效降解DON(150μM),表明三种辅因子对DON降解具有协同作用。所有这些结果表明Pe DDH在控制DON污染方面具有巨大潜力。

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本文引用的文献

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从西藏拟青霉中鉴定和应用一种新型脱氧雪腐镰刀菌烯醇降解酶。
Food Chem. 2024 Mar 1;435:137609. doi: 10.1016/j.foodchem.2023.137609. Epub 2023 Sep 29.
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Improvement of catalytic activity of sorbose dehydrogenase for deoxynivalenol degradation by rational design.通过合理设计提高山梨醇脱氢酶对脱氧雪腐镰刀菌烯醇降解的催化活性。
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Structure-function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenol.醛酮还原酶解毒真菌毒素脱氧雪腐镰刀烯醇的结构功能特征。
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