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Analysis of laccase-like enzymes secreted by fungi isolated from a cave in Northern Spain
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  • Daniel Fernández-Remacha,
  • Candela González-Riancho,
  • Miranda Lastra Osua,
  • Aránzazu González Arce,
  • Itxaso Montánchez,
  • Juan María García-Lobo,
  • Roger Estrada-Tejedor,
  • Vladimir Kaberdin
Daniel Fernández-Remacha
Universitat Ramon Llull

Corresponding Author:[email protected]

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Candela González-Riancho
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Miranda Lastra Osua
University of the Basque Country - Bizkaia Campus
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Aránzazu González Arce
University of the Basque Country - Bizkaia Campus
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Itxaso Montánchez
University of the Basque Country - Bizkaia Campus
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Juan María García-Lobo
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Roger Estrada-Tejedor
Universitat Ramon Llull
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Vladimir Kaberdin
University of the Basque Country - Bizkaia Campus
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Laccases belong to a family of multicopper enzymes able to oxidize a broad spectrum of organic compounds. Despite the well-known property of laccases to carry out bleaching and degradation of industrial dyes and polyphenolic compounds, their industrial use is often limited by the high cost, low efficiency, or instability of these enzymes. To look for new microorganisms which produce laccases that are potentially suitable for industrial applications, we have isolated several fungal strains from a cave in northern Spain. Their phenotypic analysis on agar plates supplemented with ABTS (2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)) disclosed two laccase-positive strains. Further genotyping revealed that they belonged to the Gliomastix murorum and Conidiobolus thromboides species. The secretion of G. murorum and C. thromboides laccase-like enzymes was then confirmed by zymography. Further identification of these polypeptides by mass-spectroscopy revealed the nature of the laccases and made it possible to predict their functional domains and other features. In addition, plate assays revealed that the laccases secreted by both G. murorum and C. thromboides were capable of degrading industrial dyes (Congo Red, Indigo, and Eriochrome Black T). Homology modeling and substrate docking predicted the putative structure of the currently uncrystallized G. murorum enzyme as well as its amino acid residues potentially involved in interactions with these dyes. In summary, new biochemical and structural insights into decolorization mediated by G. murorum laccase as well as identification of laccase-like oxidase in C. thromboides point to a promising future for these enzymes in biotechnology.
23 Oct 2021Submitted to MicrobiologyOpen
25 Oct 2021Submission Checks Completed
25 Oct 2021Assigned to Editor
30 Oct 2021Reviewer(s) Assigned
25 Nov 2021Review(s) Completed, Editorial Evaluation Pending
26 Nov 2021Editorial Decision: Revise Minor
10 Feb 20221st Revision Received
11 Feb 2022Assigned to Editor
11 Feb 2022Submission Checks Completed
11 Feb 2022Review(s) Completed, Editorial Evaluation Pending
11 Feb 2022Reviewer(s) Assigned
08 Mar 2022Editorial Decision: Revise Minor
12 Mar 20222nd Revision Received
14 Mar 2022Assigned to Editor
14 Mar 2022Submission Checks Completed
14 Mar 2022Review(s) Completed, Editorial Evaluation Pending
16 Mar 2022Editorial Decision: Accept