Literature DB >> 18685269

Fungal enzymes for environmental purposes, a molecular biology challenge.

Marcela Ayala1, Michael A Pickard, Rafael Vazquez-Duhalt.   

Abstract

In their capacity to transform xenobiotics and polluting compounds, fungal peroxidases and their use in the environmental field have a recognized and important potential. However, both fundamental and practical issues, such as enzyme stability and availability, have delayed the development of industrial applications. Three main protein engineering challenges have been identified: (1) Enhancement of operational stability, specifically hydrogen peroxide stability in the case of fungal peroxidases. (2) Increase of the enzyme redox potential in order to widen the substrate range. (3) Development of heterologous expression and industrial production. The bottlenecks, advances and strategies that have been proven successful are discussed. Copyright 2008 S. Karger AG, Basel.

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Year:  2008        PMID: 18685269     DOI: 10.1159/000121328

Source DB:  PubMed          Journal:  J Mol Microbiol Biotechnol        ISSN: 1464-1801


  5 in total

1.  Laccase encapsulation in chitosan nanoparticles enhances the protein stability against microbial degradation.

Authors:  Rina D Koyani; Rafael Vazquez-Duhalt
Journal:  Environ Sci Pollut Res Int       Date:  2016-06-18       Impact factor: 4.223

2.  Improving the oxidative stability of a high redox potential fungal peroxidase by rational design.

Authors:  Verónica Sáez-Jiménez; Sandra Acebes; Victor Guallar; Angel T Martínez; Francisco J Ruiz-Dueñas
Journal:  PLoS One       Date:  2015-04-29       Impact factor: 3.240

3.  Engineering a fungal peroxidase that degrades lignin at very acidic pH.

Authors:  Elena Fernández-Fueyo; Francisco J Ruiz-Dueñas; Angel T Martínez
Journal:  Biotechnol Biofuels       Date:  2014-07-24       Impact factor: 6.040

4.  Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase.

Authors:  Verónica Sáez-Jiménez; Elena Fernández-Fueyo; Francisco Javier Medrano; Antonio Romero; Angel T Martínez; Francisco J Ruiz-Dueñas
Journal:  PLoS One       Date:  2015-10-23       Impact factor: 3.240

5.  Exploring the Role of Phenylalanine Residues in Modulating the Flexibility and Topography of the Active Site in the Peroxygenase Variant PaDa-I.

Authors:  Joaquin Ramirez-Ramirez; Javier Martin-Diaz; Nina Pastor; Miguel Alcalde; Marcela Ayala
Journal:  Int J Mol Sci       Date:  2020-08-10       Impact factor: 5.923

  5 in total

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