Structure-based Engineering of a Plant-Fungal Hybrid Peroxidase for Enhanced Temperature and pH Tolerance

Cell Chem Biol. 2018 Aug 16;25(8):974-983.e3. doi: 10.1016/j.chembiol.2018.04.014. Epub 2018 May 24.

Abstract

In an age of ever-increasing biotechnological and industrial demand for new and specialized biocatalysts, rational protein engineering offers a direct approach to enzyme design and innovation. Heme peroxidases, as indispensable oxidative biocatalysts, provide a relatively mild alternative to the traditional harsh, and often toxic, chemical catalysts, and subsequently, have found widespread application throughout industry. However, the potential for these enzymes is far greater than their present use, as processes are currently restricted to the more stable, but less catalytically powerful, subset of peroxidases. Here we describe the structure-guided, rational engineering of a plant-fungal hybrid peroxidase built to overcome the application barrier of these high-reduction potential peroxidases. This engineered enzyme has the catalytic versatility and oxidative ability of a high-reduction potential versatile peroxidase, with enhanced temperature and pH tolerance similar to that of a highly stable plant peroxidase.

Keywords: biocatalysis; biofuels; enzyme engineering; enzymes; lignin; oxidation; peroxidases.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biotechnology
  • Enzyme Stability
  • Escherichia coli / genetics
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Oxidation-Reduction
  • Peroxidase / chemistry*
  • Peroxidase / genetics*
  • Peroxidase / metabolism
  • Plants / chemistry
  • Plants / enzymology*
  • Plants / genetics
  • Plants / metabolism
  • Pleurotus / chemistry
  • Pleurotus / enzymology*
  • Pleurotus / genetics
  • Pleurotus / metabolism
  • Protein Conformation
  • Protein Engineering / methods*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Substrate Specificity
  • Temperature

Substances

  • Recombinant Fusion Proteins
  • Peroxidase