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Carbohydrate-Active Enzymes—a Tribute to Peter Biely and His Contribution to Science

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Macromolecular Chemistry".

Deadline for manuscript submissions: closed (1 May 2022) | Viewed by 6975

Special Issue Editors


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Guest Editor
1. School of Agriculture, Food and Wine, University of Adelaide, Adelaide, SA 5064, Australia
2. School of Life Science, Huaiyin Normal University, Huai’an 223300, China
Interests: bioinformatics; biotechnology; enzymology; molecular modeling; plant transport proteins; protein structure-function; synthetic biology; X-ray crystallography
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden
Interests: biomass fractionation; biomass processing with biocatalysis; biocatalytic CO2 capture and conversion
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Guest Editor
Department of Microbiology, Faculty of Biology, University of Barcelona, SpainInstitute of Nanoscience and Nanotechnology (IN2UB), University of Barcelona, Barcelona, Spain
Interests: biomass degradation; biotechnology; enzymology; paper technology; xylanases

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Guest Editor
Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 9 Iroon Polytech Str, Zografou Campus, 15780 Athens, Greece
Interests: biocatalysis; industrial biotechnology; lignocellulose degrading enzymes; novel enzymes; structure-function relationship
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Plant biomass is an important renewable resource. The economic feasibility of the process of its bioconversion to biofuels, biochemicals and other high-value products is accentuated by the complexity of the structure of plant cell walls and simultaneously hampered by the insufficient knowledge of their biosynthesis and degradation. The reason for this is evolution, which changes the characteristics of species and relies on the process of natural selection. The pressure from microorganisms confronting plant biomass leads to the formation of plant cell wall structures that echo plant responses to the environment. Nevertheless, the pressure on microorganisms to survive allows for the progression of novel biocatalysts cleaving most of the covalent linkages contained in plant cell walls. This issue is focused on carbohydrate-active enzymes involved in the biodegradation of plant cell walls with a special emphasis on plant polysaccharides and enzyme catalytic mechanisms. This knowledge aims to contribute to the progress towards the bioconversion of plant biomass.

We wish to dedicate this Special Issue to Dr. Peter Biely, a chief scientist at the Institute of Chemistry of the Slovak Academy of Sciences, on the occasion of his 80th birthday. Dr. Biely is a true research pioneer in the field of carbohydrate-active enzymes, who has made immense contributions to the field. His advances on the elucidation of catalytic function and the mode of action of specifically xylan-degrading enzymes, using classic biochemical approaches, have been ground-breaking.

Contributions on any aspect of this field are welcome, such as biochemical and biophysical analyses, structural studies, structure–function relationships, computational approaches, and applications of analyzed enzymes, and are not limited to the following:

  • Biofuels and biochemicals;
  • Carbohydrate-active enzymes;
  • Carbohydrate esterases;
  • Catalytic mechanisms;
  • Computational chemistry;
  • Enzyme bioengineering;
  • Glycoside hydrolases and transferases;
  • Plant cell walls;
  • Plant polysaccharides;
  • Structure–function relationships.

Prof. Dr. Maria Hrmova
Prof. Dr. Paul Christakopoulos
Prof. Dr. Francisco I. Javier Pastor
Dr. Evangelos Topakas
Guest Editors

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 submissions that pass pre-check are 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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 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

  • Applications
  • Bioengineering
  • Biofuels
  • Biomass
  • Enzymatic hydrolysis
  • Microbial degradation
  • NMR spectroscopy
  • Structure-based enzyme design
  • Structure–function
  • Substrate specificity
  • X-ray crystallography

Published Papers (3 papers)

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Editorial

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4 pages, 189 KiB  
Editorial
Special Issue: “Peter Biely, A Pioneering Researcher in the Enzymology of Plant Biomass Degradation”
by Maria Hrmova
Molecules 2021, 26(16), 4857; https://doi.org/10.3390/molecules26164857 - 11 Aug 2021
Viewed by 1648
Abstract
As it has been outlined on the website of the Special Issue entitled “Peter Biely, a pioneering researcher in the enzymology of plant biomass degradation” in the journal Molecules (section Macromolecular Chemistry, ISSN 1420-3049), plant biomass is a key renewable resource [...] Full article

Research

Jump to: Editorial

15 pages, 3109 KiB  
Article
Elucidating Sequence and Structural Determinants of Carbohydrate Esterases for Complete Deacetylation of Substituted Xylans
by Leena Penttinen, Vera Kouhi, Régis Fauré, Tatiana Skarina, Peter Stogios, Emma Master and Edita Jurak
Molecules 2022, 27(9), 2655; https://doi.org/10.3390/molecules27092655 - 20 Apr 2022
Cited by 3 | Viewed by 2204
Abstract
Acetylated glucuronoxylan is one of the most common types of hemicellulose in nature. The structure is formed by a β-(1→4)-linked D-xylopyranosyl (Xylp) backbone that can be substituted with an acetyl group at O-2 and O-3 positions, and α-(1→2)-linked [...] Read more.
Acetylated glucuronoxylan is one of the most common types of hemicellulose in nature. The structure is formed by a β-(1→4)-linked D-xylopyranosyl (Xylp) backbone that can be substituted with an acetyl group at O-2 and O-3 positions, and α-(1→2)-linked 4-O-methylglucopyranosyluronic acid (MeGlcpA). Acetyl xylan esterases (AcXE) that target mono- or doubly acetylated Xylp are well characterized; however, the previously studied AcXE from Flavobacterium johnsoniae (FjoAcXE) was the first to remove the acetyl group from 2-O-MeGlcpA-3-O-acetyl-substituted Xylp units, yet structural characteristics of these enzymes remain unspecified. Here, six homologs of FjoAcXE were produced and three crystal structures of the enzymes were solved. Two of them are complex structures, one with bound MeGlcpA and another with acetate. All homologs were confirmed to release acetate from 2-O-MeGlcpA-3-O-acetyl-substituted xylan, and the crystal structures point to key structural elements that might serve as defining features of this unclassified carbohydrate esterase family. Enzymes comprised two domains: N-terminal CBM domain and a C-terminal SGNH domain. In FjoAcXE and all studied homologs, the sequence motif around the catalytic serine is Gly-Asn-Ser-Ile (GNSI), which differs from other SGNH hydrolases. Binding by the MeGlcpA-Xylp ligand is directed by positively charged and highly conserved residues at the interface of the CBM and SGNH domains of the enzyme. Full article
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13 pages, 4449 KiB  
Article
Yeast GH30 Xylanase from Sugiyamaella lignohabitans Is a Glucuronoxylanase with Auxiliary Xylobiohydrolase Activity
by Katarína Šuchová, Andrej Chyba, Zuzana Hegyi, Martin Rebroš and Vladimír Puchart
Molecules 2022, 27(3), 751; https://doi.org/10.3390/molecules27030751 - 25 Jan 2022
Cited by 5 | Viewed by 2010
Abstract
Xylanases are the enzymes that catalyze the breakdown of the main hemicellulose present in plant cell walls. They have attracted attention due to their biotechnological potential for the preparation of industrially interesting products from lignocellulose. While many xylanases have been characterized from bacteria [...] Read more.
Xylanases are the enzymes that catalyze the breakdown of the main hemicellulose present in plant cell walls. They have attracted attention due to their biotechnological potential for the preparation of industrially interesting products from lignocellulose. While many xylanases have been characterized from bacteria and filamentous fungi, information on yeast xylanases is scarce and no yeast xylanase belonging to glycoside hydrolase (GH) family 30 has been described so far. Here, we cloned, expressed and characterized GH30 xylanase SlXyn30A from the yeast Sugiyamaella lignohabitans. The enzyme is active on glucuronoxylan (8.4 U/mg) and rhodymenan (linear β-1,4-1,3-xylan) (3.1 U/mg) while its activity on arabinoxylan is very low (0.03 U/mg). From glucuronoxylan SlXyn30A releases a series of acidic xylooligosaccharides of general formula MeGlcA2Xyln. These products, which are typical for GH30-specific glucuronoxylanases, are subsequently shortened at the non-reducing end, from which xylobiose moieties are liberated. Xylobiohydrolase activity was also observed during the hydrolysis of various xylooligosaccharides. SlXyn30A thus expands the group of glucuronoxylanases/xylobiohydrolases which has been hitherto represented only by several fungal GH30-7 members. Full article
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