Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutation, food-grade expression, and characterization of a lactonase for zearalenone degradation.

Applied microbiology and biotechnology - 1 Aug 2023

Qiu Yangyu, Xu Huidong, Ji Qinyi, Xu Rongrong, Zhu Mulan, Dang Yali, Shi Xizhi, Zhang Lili, Xia Yu

Abstract excerpt

Zearalenone (ZEN) is a mycotoxin that causes serious threats to human health. People are exposed to ZEN contamination externally and internally through many ways, while environmental-friendly strategies for efficient elimination of ZEN are urgently needed worldwide. Previous studies revealed that the lactonase Zhd101 from Clonostachys rosea can hydrolyze ZEN to low toxicity compounds. In this work, the enzyme...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Mutation
Share to Mycotoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 37401996
DOI: 10.1007/s00253-023-12638-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation, food-grade expression, and characterization of a lactonase for zearalenone degradation.PMID 37401996Read ↗

Identification of a Potent Enzyme for the Detoxification of Zearalenone.Semantic proximity Read ↗

Enhancing the Thermostability and Catalytic Activity of a Multicopper Oxidase from Bacillus megaterium for Aflatoxin B1 and Zearalenone Degradation.Semantic proximity Read ↗

Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis.Semantic proximity Read ↗

Isolation and characterization of a Bacillus licheniformis strain capable of degrading zearalenoneSemantic proximity Read ↗

Biochemical Characterization and Mutational Analysis of a Lactone Hydrolase from Phialophora americana.Semantic proximity Read ↗

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin ZearalenoneSemantic proximity Read ↗

Expression of the Clonostachys rosea lactonohydrolase gene by Lactobacillus reuteri to increase its zearalenone-removing abilitySemantic proximity Read ↗

Isolation and characterization of a Bacillus amyloliquefaciens strain with zearalenone removal ability and its probiotic potential.Semantic proximity Read ↗

Multi-pronged design enhances thermostability of zearalenone hydrolase ZenR for enzymatic detoxification of maize flour.Semantic proximity Read ↗

Identification and rational engineering of a novel zearalenone-degrading enzyme from Fonsecaea erecta.Semantic proximity Read ↗

Cryptococcus podzolicus Y3 degrades ochratoxin A by intracellular enzymes and simultaneously eliminates citrininSemantic proximity Read ↗

Characterization and site-directed mutation of a novel aldo-keto reductase from Lodderomyces elongisporus NRRL YB-4239 with high production rate of ethyl (R)-4-chloro-3-hydroxybutanoate.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.