Biochemical characterization of Serpula lacrymans iron-reductase enzymes in lignocellulose breakdown

Author:

Nurika Irnia1,Eastwood Daniel C2,Bugg Timothy D H3,Barker Guy C4

Affiliation:

1. grid.411744.3 0000 0004 1759 2014 Department of Agroindustrial Technology, Faculty of Agricultural Technology Universitas Brawijaya 65145 Malang Indonesia

2. grid.4827.9 0000 0001 0658 8800 Department of Biosciences University of Swansea SA28PP Swansea UK

3. grid.7372.1 0000 0000 8809 1613 Department of Chemistry University of Warwick CV47AL Coventry UK

4. grid.7372.1 0000 0000 8809 1613 School of Life Sciences University of Warwick CV47AL Coventry UK

Abstract

Abstract Putative iron-reductase (IR) genes from Serpula lacrymans with similarity to the conserved iron-binding domains of cellobiose dehydrogenase (CDH) enzymes have been identified. These genes were cloned and expressed to functionally characterize their activity and role in the decomposition of lignocellulose. The results show that IR1 and IR2 recombinant enzymes have the ability to depolymerize both lignin and cellulose, are capable of the reduction of ferric iron to the ferrous form, and are capable of the degradation of nitrated lignin. Expression of these genes during wheat straw solid-state fermentation was shown to correlate with the release of compounds associated with lignin decomposition. The results suggest that both IR enzymes mediate a non-enzymatic depolymerisation of lignocellulose and highlight the potential of chelator-mediated Fenton systems in the industrial pre-treatment of biomass.

Funder

Engineering and Physical Sciences Research Council

Publisher

Oxford University Press (OUP)

Subject

Applied Microbiology and Biotechnology,Biotechnology,Bioengineering

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