Gansu Key Laboratory of Viticulture and Enology, College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, China.
Academy of State, Administration of Grain, Beijing 100032, China.
Toxins (Basel). 2019 Sep 6;11(9):518. doi: 10.3390/toxins11090518.
Ochratoxin A (OTA) is a well-known, natural contaminant in foods and feeds because of its toxic effects, such as nephrotoxicity in various animals. Recent studies have revealed that could generate enzymes to efficiently degrade OTA to ochratoxin α (OTα) in vitro. In an effort to obtain the OTA degrading mechanism, we purified and identified a novel degrading enzyme, N-acyl-L-amino acid amidohydrolase (OTase), from DSM 16503 via mass spectrometry. The same gene of the enzyme was also encountered in other strains. OTase belongs to peptidase family M20 and contains metal ions at the active site. In this study, recombination OTase was expressed and characterized in . The molecular mass of recombinant rOTase was approximately 47.0 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme exhibited a wide temperature range (30-70 °C) and pH adaptation (4.5-9.0) and the optimal temperature and pH were 50 °C and 6.5, respectively.
赭曲霉毒素 A（OTA）是一种众所周知的食品和饲料天然污染物，因其毒性作用，如各种动物的肾毒性。最近的研究表明， 可以产生酶，在体外有效地将 OTA 降解为赭曲霉毒素 α（OTα）。为了获得 OTA 降解机制，我们通过质谱法从 DSM 16503 中纯化并鉴定了一种新型的降解酶，N-酰基-L-氨基酸酰胺水解酶（OTase）。该酶的相同基因也存在于其他 菌株中。OTase 属于肽酶家族 M20，在活性位点含有金属离子。在这项研究中，重组 OTase 在 中表达和表征。重组 rOTase 的分子量约为 47.0 kDa，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）测定。该酶表现出较宽的温度范围（30-70°C）和 pH 适应范围（4.5-9.0），最佳温度和 pH 值分别为 50°C 和 6.5。
