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.

中文翻译：

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木质纤维素分解中Serpula lacrymans铁还原酶的生化特征。

已经鉴定出来自Serpula lacrymans的推定铁还原酶（IR）基因与纤维二糖脱氢酶（CDH）酶的保守铁结合域相似。克隆并表达这些基因，以在功能上表征其活性和木质纤维素分解中的作用。结果表明，IR1和IR2重组酶具有使木质素和纤维素解聚的能力，能够将三价铁还原为亚铁形式，并且能够降解硝化的木质素。这些基因在小麦秸秆固态发酵过程中的表达与木质素分解相关化合物的释放相关。