ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Discovery to Engineering of Mycotoxin Deoxynivalenol Degrading Enzymes Based on the Specialized Glyoxalase I.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- FireProtASR 2.0: evolution-guided Design of Protein Ancestors and Successors with phylogenetics and machine learning.Briefings in bioinformatics · 2026Article
- Specialized aldo-keto reductases trigger complete degradation of mycotoxin deoxynivalenol.Nature communications · 2026Article
- Discovery to Engineering of Mycotoxin Deoxynivalenol Degrading Enzymes Based on the Specialized Glyoxalase I.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
Deoxynivalenol (DON) is a mycotoxin that is omnipresent in food and feed. Therefore, this study has focused on discovery, molecular characterization, and engineering of DON degrading enzymes, based on a DON isomerizing enzyme (e.g., the specialized glyoxalase I from Gossypium raimondii (Gr-SPG)). A molecular phylogeny-based sequence and structure analysis elucidated the evolutionary trajectory of the DON degrading enzymes. Ancestral sequence reconstruction led to the generation of thermostable evolutionary intermediates of SPG (e.g., Anc216). Molecular modeling and consensus protein design allowed to understand the structure and function relationships and also identify the key conserved mutations that influence catalytic activity and thermostability. Ultimately, a highly active and thermostable SPG (e.g., a quintuple mutant of Anc216 (Anc216_M5)) was constructed from a newly discovered extant SPG enzyme (OR9). The Anc216_M5 exhibited a
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