Biotransformation of Deoxynivalenol by a Dual-Member Bacterial Consortium Isolated from Tenebrio molitor Larval Feces

Yang Wang; Donglei Zhao; Wei Zhang; Songxue Wang; Kai Huang; Baoyuan Guo

doi:10.3390/toxins15080492

Biotransformation of Deoxynivalenol by a Dual-Member Bacterial Consortium Isolated from Tenebrio molitor Larval Feces

Toxins (Basel). 2023 Aug 4;15(8):492. doi: 10.3390/toxins15080492.

Authors

Yang Wang¹, Donglei Zhao^{1

2}, Wei Zhang¹, Songxue Wang¹, Kai Huang², Baoyuan Guo^{1

2}

Affiliations

¹ Institute of Grain and Oil Quality and Safety, Academy of National Food and Strategic Reserves Administration, No.11 Baiwanzhuang Street, Xicheng District, Beijing 100037, China.
² School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China.

Abstract

In this study, a dual-member bacterial consortium with the ability to oxidize deoxynivalenol (DON) to 3-keto-DON, designated SD, was first screened from the feces of Tenebrio molitor larvae. This consortium consisted of Pseudomonas sp. SD17-1 and Devosia sp. SD17-2, as determined by 16S rRNA-based phylogenetic analysis. A temperature of 30 °C, a pH of 8.0-9.0, and an initial inoculum concentration ratio of Devosia to Pseudomonas of 0.1 were optimal single-factor parameters for the DON oxidation activity of the bacterial consortium SD. Genome-based bioinformatics analysis revealed the presence of an intact PQQ biosynthesis operon (pqqFABCDEG) and four putative pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase (ADH) genes in the genomes of Pseudomonas strain SD17-1 and Devosia strain SD17-2, respectively. Biochemical analyses further confirmed the PQQ-producing phenotype of Pseudomonas and the DON-oxidizing enzymatic activities of two of four PQQ-dependent ADHs in Devosia. The addition of PQQ-containing a cell-free fermentation supernatant from Pseudomonas activated DON-oxidizing activity of Devosia. In summary, as members of the bacterial consortium SD, Pseudomonas and Devosia play indispensable and complementary roles in SD's oxidation of DON. Specifically, Pseudomonas is responsible for producing the necessary PQQ cofactor, whereas Devosia expresses the PQQ-dependent DON dehydrogenase, together facilitating the oxidation of DON.

Keywords: Devosia; PQQ-dependent alcohol dehydrogenase; Pseudomonas; deoxynivalenol; transformation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Biotransformation
Feces
Larva
PQQ Cofactor
Phylogeny
Pseudomonas / genetics
RNA, Ribosomal, 16S
Tenebrio*

Substances

deoxynivalenol
RNA, Ribosomal, 16S
PQQ Cofactor

Grants and funding

This research was funded by the National Natural Science Foundation of China (Grant No. 31972605) and the Key Research and Development Program of Ningxia Hui Autonomous Region, China (Grant No. 2022BBF03031).