ArticleFolia microbiologica2022
Excavation, expression, and functional analysis of a novel zearalenone-degrading enzyme.
Article in Folia microbiologica, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- The characterization of a new stabilized lactonase from the endophytic fungi Aspergillus pseudonomiae with anti-bacterial and anti-fungal properties.Protein science : a publication of the Protein Society · 2026Article
- Identification and Thermal Stability Modification of a Zearalenone Lactone Hydrolase ZHD30L.Toxins · 2026Article
- Efficient Biotransformation of Zearalenone in Acidic Food Matrices by Alkaline Enzyme-Inorganic Hybrid Nanoflower.Toxins · 2026Article
- Efficient Expression of Lactone Hydrolase Cr2zen for Scalable Zearalenone Degradation inToxins · 2025Article
- High-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris via combinatorial strategy.Archives of microbiology · 2025Article
- Advances in zearalenone-degrading enzymes research: characteristics, mining, improvement, and application.Journal of animal science and biotechnology · 2025Review
- Green Solutions for Food Safety: The Emerging Applications of Zearalenone-Degrading Enzymes.Foods (Basel, Switzerland) · 2025Review
- Article
- Characteristics of a Novel Zearalenone Lactone Hydrolase ZHRnZ and Its Thermostability Modification.International journal of molecular sciences · 2024Article
- Bioenzymatic detoxification of mycotoxins.Frontiers in microbiology · 2024Review
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Zearalenone (ZEN) is a toxic secondary metabolite of Fusarium sp. commonly found in wheat, corn, and other crops. In addition to economic losses, ZEN can seriously endanger the health of both humans and livestock, thus presenting an urgent need for ZEN-detoxifying enzymes that function in the extreme heat or pH conditions of industrial fermenters. Here, we identify and characterize the activity of the ZEN-degrading enzyme from Exophiala spinifera, ZHD_LD, which shares 60.15% amino acid identity and a conserved catalytic triad with the well-characterized ZEN-detoxifying protein ZHD101 from Clonostachys rosea. Biochemical activity and stability assays indicated that purified recombinant ZHD_LD exhibited high activity against ZEN with optimal reaction conditions of 50 ℃ and pH 7.0-10.0. Structural modeling of the ZHD_LD active site and comparison with ZHD101 revealed its likely mechanism of ZEN degradation. This research provides an industrially valuable candidate enzyme for ZEN detoxification in food and livestock feed.
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