Discovery of a novel fungal lignin peroxidases based on genome mining
- Discovery of a novel fungal lignin peroxidases based on genome mining
- 민경선; 김세일; 우한민; Pham Le Thanh Mai; 김용환; 엄영순
- biorefinery; lignin degradation; genome mining
- Issue Date
- WCCE9 & APCChE2013
- For an efficient use of lignocellulosic biomass in biorefinery process, lignin degradation must be preceded. In nature, fungi are usually responsible for lignin degradation by secretion of lignin degrading biocatalysts. Although there are so many fungi resident in lignocellulose-rich environment, only lignin peroxidase (LiP) and manganese peroxidase (MnP) from Phanerochaete chrysosporium are commercially available and widely used for research. In this study, we aimed to discover novel fungal LiPs based on genome mining. The amino acid sequence of LiPH8 from P. chrysosporium was used as a BLASTP query against JGI fungal genomes. Seven fungal genomes were selected based on the highest BLAST hit. Based on the 3-dimensional modeling, structural alignment, and phylogenetic analysis, 6 LiP candidates were selected; LP02, LP06, LP17, LP20, LP21, and LP22. The amino acid sequence similarity of candidates to LIPH8 was 49.1 % ~ 64.6 %. LP02, LP06, and LP21 were found to have completely conserved heme binding site and Ca2+ binding site, while those binding sites of LP17, LP20, and LP22 were different from the conserved sequence by 1~2 amino acids. The 6 LiP candidate sequence were synthesized and the codon was optimized for E. coli expression. Interestingly, the synthesized LP20 genes were expressed in a soluble form, whereas LiPH8 from P. chrysosporium formed an inclusion body in E.coli. We also investigated the activity using veratryl alcohol as the substrate and LP20 successfully oxidized veratryl alcohol to veratryl aldehyde. Further characterization of LP20 and other candidates will provide more information on lignin degrading biocatalysts.
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