Thermophilic enzyme systems for efficient conversion of lignocellulose to valuable products: Structural insights and future perspectives for esterases and oxidative catalysts

Bioresour Technol. 2019 May:279:362-372. doi: 10.1016/j.biortech.2019.01.062. Epub 2019 Jan 16.

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.

Keywords: Biotransformation; Esterases; LPMOs; Laccases; Lignocellulose valorization; Peroxidases; Thermophilic enzymes; Thermostability.

Publication types

  • Review

MeSH terms

  • Animals
  • Biocatalysis
  • Esterases
  • Humans
  • Lignin / metabolism*
  • Mixed Function Oxygenases / metabolism
  • Oxidation-Reduction
  • Substrate Specificity

Substances

  • lignocellulose
  • Lignin
  • Mixed Function Oxygenases
  • Esterases