ArticleSpringerPlus2015
Functional characterization of a yellow laccase from Leucoagaricus gongylophorus.
Article in SpringerPlus, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 24 citations in OpenAlex.
- Wheat bran as an efficient agro-process waste for enhanced yellow laccase production by3 Biotech · 2024Article
- Article
- Biodegradation of anthracene and different PAHs by a yellow laccase from Leucoagaricus gongylophorus.Environmental science and pollution research international · 2019Article
- Molecular cloning, expression and characterization of poxa1b gene from Pleurotus ostreatus.Molecular biology reports · 2019Article
- Acetylcholinesterases from Leaf-Cutting antEnzyme research · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work we have identified, using mass spectrometry, two laccases produced by Leucoagaricus gongylophorus. One of them, Lac1Lg, was isolated, purified and characterized. Lac1Lg, a monomeric enzyme, was studied using ABTS and syringaldazine substrates. Lac1Lg presented kcat/Km almost threefold higher for syringaldazine than for ABTS, showing a higher catalytic efficiency of Lac1Lg for syringaldazine. The interference of several metal ions and substances in the laccase activity were evaluated. Lac1Lg did not absorb at 600 nm, which is a characteristic of so-called yellow laccases. Lac1Lg also was able to oxidize non-phenolic substrate (anthracene) in the absence of an exogenous mediator, showing that the enzyme has potential to explore in biotechnological processes. Our Lac1Lg three-dimensional molecular model, constructed using homology modeling, showed that the Lac1Lg catalytic site is very closed to blue laccases.
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Registered trials
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