Glycoside hydrolases from (hyper)thermophilic archaea: structure, function, and applications

Created 18 marca 2026

Updated on 23 czerwca 2026

approved

(Hyper)thermophilic archaeal glycosidases are enzymes that catalyze the hydrolysis of glycosidic bonds to break down complex sugars and polysaccharides at high temperatures. These enzymes have an unique structure that allows them to remain stable and functional in extreme environments such as hot springs and hydrothermal vents. This review provides an overview of the current knowledge and milestones on the structures and functions of (hyper)thermophilic archaeal glycosidases and their potential applications in various fields. In particular, this review focuses on the structural characteristics of these enzymes and how these features relate to their catalytic activity by discussing different types of (hyper)thermophilic archaeal glycosidases, including β-glucosidases, chitinase, cellulases and α-amylases, describing their molecular structures, active sites, and mechanisms of action, including their role in the hydrolysis of carbohydrates. By providing a comprehensive overview of (hyper)thermophilic archaeal glycosidases, this review aims to stimulate further research into these fascinating enzymes.

itineris-hub
Tags:
Archaea
CAZymes
Extremozymes
Glycosidases
Hyperthermophiles
Publication - Article
Basic
Język
English
MainTitle
Glycoside hydrolases from (hyper)thermophilic archaea: structure, function, and applications
Original ids
https://doi.org/10.1042/ebc20220196
Typ
publication
bestAccessRight
RESTRICTED
contributors
  • Department of Biology, University of Naples "Federico II", Complesso Universitario Di Monte S. Angelo, Via Cupa Nuova Cinthia 21, Naples, 80126, Italy;
  • Institute of Biosciences and BioResources, National Research Council of Italy, Via P. Castellino 111, Naples, 80131, Italy;
  • Task Force on Microbiome Studies, University of Naples Federico II, 80100 Naples, Italy;
  • NBFC, National Biodiversity Future Center, 90133 Palermo, Italy.
countries
Italy
Creator/Author
Full name
  • Iacono, Roberta;
  • De Lise, Federica, orcid: 0000-0002-9614-9226;
  • Moracci, Marco, orcid: 0000-0002-9846-2531;
  • Cobucci-Ponzano, Beatrice, orcid: 0000-0002-8211-2297;
  • Strazzulli, Andrea, orcid: 0000-0002-9690-149x
Other
Opis
(Hyper)thermophilic archaeal glycosidases are enzymes that catalyze the hydrolysis of glycosidic bonds to break down complex sugars and polysaccharides at high temperatures. These enzymes have an unique structure that allows them to remain stable and functional in extreme environments such as hot springs and hydrothermal vents. This review provides an overview of the current knowledge and milestones on the structures and functions of (hyper)thermophilic archaeal glycosidases and their potential applications in various fields. In particular, this review focuses on the structural characteristics of these enzymes and how these features relate to their catalytic activity by discussing different types of (hyper)thermophilic archaeal glycosidases, including β-glucosidases, chitinase, cellulases and α-amylases, describing their molecular structures, active sites, and mechanisms of action, including their role in the hydrolysis of carbohydrates. By providing a comprehensive overview of (hyper)thermophilic archaeal glycosidases, this review aims to stimulate further research into these fascinating enzymes.
Publication Date
2023-08-11
Publisher
Portland Press Ltd.
Subjects
  • Archaea;
  • CAZymes;
  • Extremozymes;
  • Glycosidases;
  • Hyperthermophiles;
  • Hot Temperature;
  • Glycoside Hydrolases;
isGreen
false
isInDiamondJournal
false
Software
Publication
Ending page
751
Nazwa
Essays in Biochemistry
Publication
Article
Starting page
731
iss
4
issnOnline
1744-1358
issnPrinted
0071-1365
vol
67
Other Research Product
Detailed informations
system:type
Research Product
Management Info
Autor
Catalogue Manager ITINERIS
Wersja
1
Last Updated
czerwca 23, 2026, 11:12 (UTC)
Created
marca 18, 2026, 23:30 (UTC)
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