Enzymtechnik
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Abstrakt

Transcriptome Based Analysis of a Lentinus squarrosulus Strain for the Lignolytic Versatile Peroxidases

Aarthi Ravichandran, Manpal Sridhar, Atul P Kolte, Arindham Dhali and Shanubhoganahalli Maheswarappa Gopinath

Versatile peroxidase, an extracellular heme protein of the lignolytic system is endowed with polyvalent catalytic sites that render this protein a very high redox potential. Versatile peroxidase is regarded as a hybrid of lignin peroxidase and manganese peroxidase as this enzyme possesses the catalytic features of both these enzymes in oxidation of aromatic compounds and is a potential biocatalyst with relevance in multitude of biotechnological applications. Transcriptomic analysis of Lentinus squarrosulus demonstrated the expression of versatile peroxidase besides a plethora of biomass degrading enzymes. Bioinformatic analysis identified ten putative versatile peroxidase transcripts with significant protein sequence similarity to the versatile peroxidase isoforms of other white-rot basidiomycetes. The enzyme was purified and visualized on Sodium Dodecyl-Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) with a molecular weight of 49 KDa. Further, application of this purified enzyme on lignocellulosic crop residues showed remarkable decrease in lignin content with corresponding increase of 18-20% in vitro dry matter digestibility. Transcriptome analysis of L.squarrosulus revealed significant facts about the biodegradative ability of this fungus potentially paving the way for efficient biotechnological applications utilizing its potency