Insights into the Mechanism of Lignocellulose Degradation by Versatile Peroxidases

Abstract

Lignocelluloses are imperative structural components of plant cell wall and are profusely found in agricultural crop residues. The structural heterogeneity and recalcitrance of lignin limit the accessibility of cell wall carbohydrates for constructive exploitation. During the past decades, diverse lignin degrading enzymes were characterized to facilitate the utilization of lignocellulosic biomass for technological applications. Versatile peroxidases are unique among ligninolytic enzymes for their remarkably high redox potential and ability to oxidize lignin without the requisite of redox mediators. The hybrid structural architecture of this enzyme bearing functional features of lignin peroxidase and manganese peroxidase demonstrates its versatility in aromatics oxidation. This review summarizes the distinctive structural aspects of fungal versatile peroxidase in correlation to its oxidation of aromatic substrates besides emphasizing on the catalytic environment conducive for substrate oxidation. This review also focuses on the general strategies employed for production of this enzyme, its molecular framework, potential biotechnological applications of versatile peroxidase and prospects on enhancing the production of enzyme. Finally, the significance of this enzyme in improving the nutritive value of crop residues to promote ruminal productivity is highlighted.

Purification and characterization of versatile peroxidase from Lentinus squarrosulus and its application in biodegradation of lignocellulosics

“…Activated Versatile Peroxidase has oxo ferryl (Fe 4+ ) heme hence failed to oxidize the dye. 6 Addition of manganese to this activated Versatile Peroxidase produced blue color signifying catalytic conversion of Mn 2+ to Mn 3+ by the enzyme. Manganese oxidation by peroxidases can be exemplified through this method.…”

“…A noteworthy feature is the catalysis by this enzyme unconditional of the redox mediators that is a major advantage for economic biotechnological applications. 6 Accordingly, this study was carried out to understand the kinetics and catalytic potential of a novel Versatile Peroxidase(VP)from Lentinus squarrosulus. Lentinus squarrosulus is a tropical white-rot that predominantly produces Laccase (Lac) and VP in manganese deficient medium.…”

Biochemical features of dye‐decolorizing peroxidases: Current impact on lignin degradation

“…Previous reports have highlighted a role of several different classes of enzymes in attacking lignin or lignin model compounds. Lignin peroxidases [25][26][27][28], manganese-dependent peroxidases [29][30][31], versatile peroxidases [32], and laccases [13,[33][34][35][36] have been extensively studied for their lignin degradation activity. These enzymes, except for laccases, all depend on H 2 O 2 for their activity.…”

Biotransformation of industrial tannins by filamentous fungi

“…The role of peroxidases in tannins transformation has been mostly unexplored, even though they are recognized among the most powerful fungal enzymes. Despite the redox potential of peroxidases falls in the range of 1100-1500 mV, significantly higher than laccases, stability issues mostly limited their application (Ravichandran and Sridhar 2017). Post-translational modifications are under study to enhance this feature (Sáez-Jiménez et al 2015).…”