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


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.

SUBMITTER: Nurika I 

PROVIDER: S-EPMC6971154 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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

Nurika Irnia I   Eastwood Daniel C DC   Bugg Timothy D H TDH   Barker Guy C GC  

Journal of industrial microbiology & biotechnology 20191116 1


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 capabl  ...[more]

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