1887

Abstract

A novel ligninolytic peroxidase gene () was cloned and characterized from a poroid brown-rot fungus, . The genomic DNA of the fungus harboured two copies of , with a length of 2111 bp, interlaced with 12 introns, while the full-length cDNA was 1183 bp, with a 66 bp signal peptide and an ORF of 990 bp. The three-dimensional molecular structure model was comparable to that of the versatile peroxidase of . was cloned into vector pQE31, successfully expressed in strain M15 under the control of the T5 promoter and produced a non-glycosylated protein of about 38 kDa, pI 5.42. The native and recombinant ACLnP was capable of oxidizing the redox mediator veratryl alcohol, and also decolorized bromophenol blue and 2,6-dimethoxyphenol dyes, implicating a functional extracellular peroxidase activity. The significance of discovering a functional gene in in terms of wood degradation and colonization capacity in its unique niche is discussed.

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2009-02-01
2021-01-24
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