select ad.sno,ad.journal,ad.title,ad.author_names,ad.abstract,ad.abstractlink,j.j_name,vi.* from articles_data ad left join journals j on j.journal=ad.journal left join vol_issues vi on vi.issue_id_en=ad.issue_id where ad.sno_en='102878' and ad.lang_id='3' and j.lang_id='3' and vi.lang_id='3'
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