4.6 Article

Non-enzymatic Transformation of Aflatoxin B1 by Pseudomonas geniculata m29

Journal

FRONTIERS IN MICROBIOLOGY
Volume 12, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2021.724103

Keywords

aflatoxin B-1; Pseudomonas geniculata m29; transformation; non-enzymatic; LC-MS analysis

Categories

Funding

  1. Natural Science Foundation of Anhui Province [2008085MC60]
  2. Key Program of 13th Five-Year Plan, Hefei Institutes of Physical Science, Chinese Academy of Sciences [kp-2019-21]

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A high-efficiency Pseudomonas strain m29 capable of transforming AFB(1) was isolated, with a transformation rate of over 97% within 24 hours and an optimum transformation temperature of 37 degrees Celsius. The AFB(1) transformation activity was mainly attributed to the cell-free supernatant of strain m29 and likely involved the metabolites 1,2-dimethylhydrazine or 1,1-dimethylhydrazine. This study represents the first investigation on non-enzymatic AFB(1) transformation by bacteria, with potential universal applicability to various microorganisms.
Aflatoxin B-1 (AFB(1)) is the most harmful mycotoxin produced by filamentous fungi and presents a serious threat to human and animal health. Therefore, it is essential to protect humans and animals from AFB(1)-induced acute and chronic toxicity. In this study, Pseudomonas strain m29 having a high efficiency of AFB(1) transformation was isolated from soil. The transformation ratio by m29 was more than 97% within 24 h, and the optimum temperature for transformation was 37 degrees C. Moreover, the AFB(1) transforming activity was mainly attributed to the cell-free supernatant of strain m29. The metabolite that plays a crucial role in AFB(1) transformation is likely 1,2-dimethylhydrazine or 1,1-dimethylhydrazine, as identified by GC-MS and LC-MS analysis. AFB(1) was transformed into a product with molecular formula C17H14O7. To the best of our knowledge, this is the first study of non-enzymatic AFB(1) transformation by bacteria. Importantly, this AFB(1) transformation mechanism could be universal to various microorganisms.

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