Special Issue "Lytic Polysaccharide Monooxygenases: Diversity and Molecular Events"

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".

Deadline for manuscript submissions: 30 June 2021.

Special Issue Editor

Prof. Katja Salomon Johansen
E-Mail Website
Guest Editor
Department of Geosciences and Natural Resource Management, Faculty of Science, University of Copenhagen, 1958 Copenhagen, Denmark
Interests: plant cell wall degrading enzymes; industrial biotechnology; protein chemistry; lytic polysaccharide monooxygenases

Special Issue Information

Dear Colleagues,

Lytic polysaccharide monooxygenases (LPMOs) are mononuclear copper enzymes that catalyze the oxidative cleavage of glycosidic bonds. They are characterized by two histidine residues that coordinate copper in a configuration termed the Cu-histidine brace. Although first identified in bacteria and fungi, LPMOs have since been found in all biological kingdoms. LPMOs are now included in commercial enzyme cocktails used in industrial biorefineries. This has led to increased process yield due to the synergistic action of LPMOs with glycoside hydrolases. However, the introduction of LPMOs makes control of the enzymatic step in industrial stirred-tank reactors more challenging, and the operational stability of the enzymes is reduced. It is clear that much is still to be learned about the interaction between LPMOs and their complex natural and industrial environments, and fundamental scientific studies are required toward this end. Several atomic-resolution structures have been solved providing detailed information on the Cu-coordination sphere and the interaction with the polysaccharide substrate. However, the molecular mechanisms of LPMOs are still the subject of intense investigation, the key question being how the proteinaceous environment controls the copper cofactor toward activation of the O–O bond in O2 and cleavage of the glycosidic bonds in polysaccharides. This Special Issue will focus on characterization of LPMOs and the molecular events involved in catalysis.

Prof. Katja Salomon Johansen
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • catalytic mechanism
  • roles in biological
  • structure-function
  • biotechnological application

Published Papers

This special issue is now open for submission.
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