ISSN: 2329-6674
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
Published Date: 2023-08-10; Received Date: 2023-07-10