Biodegradation Mechanisms of Patulin in Candida guilliermondii: An iTRAQ-Based Proteomic Analysis

Patulin, a potent mycotoxin, contaminates fruits and derived products worldwide, and is a serious health concern. Several yeast strains have shown the ability to effectively degrade patulin. However, the mechanisms of its biodegradation still remain unclear at this time. In the present study, biodeg...

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Bibliographic Details
Published in:Toxins 2017-02, Vol.9 (2), p.48-48
Main Authors: Chen, Yong, Peng, Huai-Min, Wang, Xiao, Li, Bo-Qiang, Long, Man-Yuan, Tian, Shi-Ping
Format: Article
Language:English
Subjects:
Biodegradation
Biodegradation, Environmental
Biological activity
Candida - classification
Candida - genetics
Candida - growth & development
Candida - metabolism
Candida guilliermondii
Cell culture
Chromatography, Liquid
Computational Biology
Contamination
Databases, Protein
Detoxification
Food Microbiology
Fruits
Fungal Proteins - genetics
Fungal Proteins - metabolism
Furans - metabolism
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Fungal
Inactivation, Metabolic
Microbial Viability
mRNA
Mycotoxins
Oxidoreductases - genetics
Oxidoreductases - metabolism
Patulin
Patulin - metabolism
Penicillium
Peptide Mapping
Proteins
Proteomics - methods
Tandem Mass Spectrometry
Time Factors
Yeast
Yeasts
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Summary:Patulin, a potent mycotoxin, contaminates fruits and derived products worldwide, and is a serious health concern. Several yeast strains have shown the ability to effectively degrade patulin. However, the mechanisms of its biodegradation still remain unclear at this time. In the present study, biodegradation and involved mechanisms of patulin by an antagonistic yeast were investigated. The results indicated that was capable of not only multiplying to a high population in medium containing patulin, but also effectively reducing patulin content in culture medium. Degradation of patulin by was dependent on the yeast cell viability, and mainly occurred inside cells. E-ascladiol was the main degradation product of patulin. An iTRAQ-based proteomic analysis revealed that the responses of to patulin were complex. A total of 30 differential proteins involved in 10 biological processes were identified, and more than two-thirds of the differential proteins were down-accumulated. Notably, a short-chain dehydrogenase (gi|190348612) was markedly induced by patulin at both the protein and mRNA levels. Our findings will provide a foundation to help enable the commercial development of an enzyme formulation for the detoxification of patulin in fruit-derived products.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins9020048