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Thermophilic enzyme systems for efficient conversion of lignocellulose to valuable products: Structural insights and future perspectives for esterases and oxidative catalysts
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-7754-9398
Biotechnology Laboratory, Department of Synthesis and Development of Industrial Processes, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
Section of Process and Environmental Engineering, Department of Chemical Engineering, University of Patras, Patras, Greece.
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2019 (English)In: Bioresource Technology, ISSN 0960-8524, E-ISSN 1873-2976, Vol. 279, p. 362-372Article in journal (Refereed) Published
Abstract [en]

Thermophilic enzyme systems are of major importance nowadays in all industrial processes due to their great performance at elevated temperatures. In the present review, an overview of the current knowledge on the properties of thermophilic and thermotolerant carbohydrate esterases and oxidative enzymes with great thermostability is provided, with respect to their potential use in biotechnological applications. A special focus is given to the lytic polysaccharide monooxygenases that are able to oxidatively cleave lignocellulose through the use of oxygen or hydrogen peroxide as co-substrate and a reducing agent as electron donor. Structural characteristics of the enzymes, including active site conformation and surface properties are discussed and correlated with their substrate specificity and thermostability properties.

Place, publisher, year, edition, pages
Elsevier, 2019. Vol. 279, p. 362-372
Keywords [en]
Thermophilic enzymes, Thermostability, Esterases, Laccases, Peroxidases, LPMOs, Biotransformation, Lignocellulose valorization
National Category
Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-73041DOI: 10.1016/j.biortech.2019.01.062ISI: 000458999200043PubMedID: 30685134Scopus ID: 2-s2.0-85060269655OAI: oai:DiVA.org:ltu-73041DiVA, id: diva2:1292188
Note

Validerad;2019;Nivå 2;2019-02-27 (johcin)

Available from: 2019-02-27 Created: 2019-02-27 Last updated: 2019-03-08Bibliographically approved

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Karnaouri, Anthi C.Antonopoulou, IoTopakas, EvangelosRova, UlrikaChristakopoulos, Paul

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