Ribonucleoside Diphosphate Reductase Plays an Important Role in Patulin Degradation by Enterobacter cloacae subsp. dissolvens.

Mengyang Xing, Boqiang Li, Yong Chen, Shiping Tian

Journal of agricultural and food chemistry 2020 May 06

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Patulin contamination is a worldwide concern due to its significant impact on human health. Several yeast strains have been screened for patulin biodegradation; however, little information is available on bacterial strains and their mechanism of degradation. In the present study, we isolated a bacterial strain TT-09 and identified it as Enterobacter cloacae subsp. dissolvens based on the BioLog system and 16S rDNA phylogenetic analysis. The strain was demonstrated to be able to transform patulin into E-ascladiol. Isobaric tags for relative and absolute quantitation and reverse transcription quantitative polymerase chain reaction analyses provided evidence that ribonucleoside diphosphate reductase (NrdA), an important enzyme involved in DNA biosynthesis, plays a crucial role in patulin degradation. Deletion of nrdA resulted in a total loss in the ability to degrade patulin in TT-09. These results indicate a new function for NrdA in mycotoxin biodegradation. The present study provides evidence for understanding a new mechanism of patulin degradation and information that can be used to develop new approaches for managing patulin contamination.

Citation

Mengyang Xing, Boqiang Li, Yong Chen, Shiping Tian. Ribonucleoside Diphosphate Reductase Plays an Important Role in Patulin Degradation by Enterobacter cloacae subsp. dissolvens. Journal of agricultural and food chemistry. 2020 May 06;68(18):5232-5240