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

Direct evolution of an alkaline fungal laccase to degrade tetracyclines.

International journal of biological macromolecules - 1 Oct 2024

Xu Jie, Zhang Yinliang, Zhu Xuelin, Shen Chen, Liu Shenglong, Xiao Yazhong, Fang Zemin

Abstract excerpt

A fungal laccase-mediator system capable of high effectively oxidizing tetracyclines under a wide pH range will benefit environmental protection. This study reported a directed evolution of a laccase PIE5 to improve its performance on tetracyclines oxidization at alkaline conditions. Two mutants, namely MutA (D229N/A244V) and MutB (N123A/D229N/A244V) were obtained. Although they shared a similar optimum pH and...

Topics

Join the communities discussing this publication.

Biodegradation, Environmental
Directed Molecular Evolution
Fungi
Hydrogen-Ion Concentration
Laccase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oxidation-Reduction

Source

Identifiers

PMID: 39111464
DOI: 10.1016/j.ijbiomac.2024.134534

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Direct evolution of an alkaline fungal laccase to degrade tetracyclines.PMID 39111464Read ↗

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

Improving the decolorization for textile dyes of a metagenome-derived alkaline laccase by directed evolution.Semantic proximity Read ↗

Widening the pH activity profile of a fungal laccase by directed evolution.Semantic proximity Read ↗

Artificial dicopper oxidase: rational reprogramming of bacterial metallo-β-lactamase into a catechol oxidase.Semantic proximity Read ↗

Coevolution of the Activity and Thermostability of an ϵ-Keto Ester Reductase for Better Synthesis of an (R)-α-Lipoic Acid Precursor.Semantic proximity Read ↗

High-Titer Production of the Fungal Anhydrotetracycline, TAN-1612, in Engineered YeastsSemantic proximity Read ↗

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

Deciphering and engineering of the final step halogenase for improved chlortetracycline biosynthesis in industrial Streptomyces aureofaciensSemantic proximity Read ↗

Focused Directed Evolution of Aryl-Alcohol Oxidase in Saccharomyces cerevisiae by Using Chimeric Signal Peptides.Semantic proximity Read ↗

Evolution of pollutant biodegradation.Semantic proximity Read ↗

Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp.Semantic proximity Read ↗

Engineering L-threonine transaldolase and a chaperone assisted cascade for the efficient biosynthesis of L-threo-p-methylsulfonylphenylserine.Semantic proximity Read ↗

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