期刊
TOXINS
卷 11, 期 9, 页码 -出版社
MDPI
DOI: 10.3390/toxins11090518
关键词
ochratoxin A; degradation; amidohydrolase; Alcaligenes faecalis; mycotoxin
资金
- National Key Research and Development Program [2017YFC1600604]
- Natural Science Foundation of Gansu Province [1506RJZA008]
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 Alcaligenes faecalis could generate enzymes to efficiently degrade OTA to ochratoxin alpha (OT alpha) 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 (AfOTase), from A. faecalis DSM 16503 via mass spectrometry. The same gene of the enzyme was also encountered in other A. faecalis strains. AfOTase belongs to peptidase family M20 and contains metal ions at the active site. In this study, recombination AfOTase was expressed and characterized in Escherichia coli. The molecular mass of recombinant rAfOTase 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 degrees C) and pH adaptation (4.5-9.0) and the optimal temperature and pH were 50 degrees C and 6.5, respectively.
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