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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.
Karnaouri, Anthi; Antonopoulou, Io; Zerva, Anastasia; Dimarogona, Maria; Topakas, Evangelos; Rova, Ulrika; Christakopoulos, Paul.
Afiliação
  • Karnaouri A; Biochemical Process Engineering, Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden. Electronic address: anthi.karnaouri@ltu.se.
  • Antonopoulou I; Biochemical Process Engineering, Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden.
  • Zerva A; Biotechnology Laboratory, Department of Synthesis and Development of Industrial Processes, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
  • Dimarogona M; Section of Process and Environmental Engineering, Department of Chemical Engineering, University of Patras, 26504 Rio, Patras, Greece.
  • Topakas E; Biotechnology Laboratory, Department of Synthesis and Development of Industrial Processes, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
  • Rova U; Biochemical Process Engineering, Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden.
  • Christakopoulos P; Biochemical Process Engineering, Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, Luleå, Sweden. Electronic address: paul.christakopoulos@ltu.se.
Bioresour Technol ; 279: 362-372, 2019 May.
Article em En | MEDLINE | ID: mdl-30685134
ABSTRACT
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Lignina Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Lignina Idioma: En Ano de publicação: 2019 Tipo de documento: Article