Catalytic activity of versatile peroxidase from Bjerkandera fumosa in aqueous solutions of water–miscible organic solvents

Rodakiewicz-Nowak, Janina; Jarosz-Wilkołazka, Anna; Luterek, Jolanta

doi:10.1016/j.apcata.2006.04.009

Cited by 33 publications

(14 citation statements)

References 28 publications

(30 reference statements)

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“…VPs have been described in species of Pleurotus and Bjerkandera (Mester and Field 1998;Kamitsuji et al 2005a, b;Pogni et al 2005;Honda et al 2006;Rodakiewicz-Nowak et al 2006). The deduced amino acid sequence of MnP2 isolated from P. ostreatus and VP (VAXPDGVNTA) from a novel strain of Bjerkandera sp.…”

Section: Enzyme System Of White Rot Fungimentioning

confidence: 94%

“…Inactivation of VP by Ca 2+ -depletion at optimum pH 4.5 due to the differences in the Fe 3+ spin states suggested that Ca 2+ -depleted VP is able to form the active intermediate compound I but its long range electron transfer is disrupted (Verdín et al 2006). The decrease in medium polarity by the addition of organic solvents like acetonitrile, dimethylsulfoxide (DMSO), ethanol, and n-propanol leads to inhibition of Bjerkandera fumosa VP (Rodakiewicz-Nowak et al 2006). Oxidizing mediators like veratryl alcohol, acetosyringone and 2,2,6,6-tetramethyl-1-piperidinyloxy (TEMPO) enhance the VP catalyzed decolorization of some textile dyes by Bjerkandera adusta (Tinoco et al 2007).…”

Section: Enzyme System Of White Rot Fungimentioning

confidence: 97%

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Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system

et al. 2008

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Increasing discharge and improper management of liquid and solid industrial wastes have created a great concern among industrialists and the scientific community over their economic treatment and safe disposal. White rot fungi (WRF) are versatile and robust organisms having enormous potential for oxidative bioremediation of a variety of toxic chemical pollutants due to high tolerance to toxic substances in the environment. WRF are capable of mineralizing a wide variety of toxic xenobiotics due to non-specific nature of their extracellular lignin mineralizing enzymes (LMEs). In recent years, a lot of work has been done on the development and optimization of bioremediation processes using WRF, with emphasis on the study of their enzyme systems involved in biodegradation of industrial pollutants. Many new strains have been identified and their LMEs isolated, purified and characterized. In this review, we have tried to cover the latest developments on enzyme systems of WRF, their low molecular mass mediators and their potential use for bioremediation of industrial pollutants.

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Section: Enzyme System Of White Rot Fungimentioning

confidence: 94%

Section: Enzyme System Of White Rot Fungimentioning

confidence: 97%

Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system

et al. 2008

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“…strain BOS55, Bjerkandera sp. (B33/3), B. fumosa, P. eryngii, P. ostreatus and P. pulmonaius, exhibit activities on aromatic substrates similar to that of LiP [189][190][191][192][193][194][195][196][197]. This group of enzymes, known as versatile peroxidases, is not only specific for Mn (II) as in MnP, but also oxidizes phenolic and non-phenolic substrates that are typical for Fig.…”

Section: Versatile Peroxidasementioning

confidence: 99%

Structure and Action Mechanism of Ligninolytic Enzymes

Wong

2008

Appl Biochem Biotechnol

723

471

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Lignin is the most abundant renewable source of aromatic polymer in nature, and its decomposition is indispensable for carbon recycling. It is chemically recalcitrant to breakdown by most organisms because of the complex, heterogeneous structure. The white-rot fungi produce an array of extracellular oxidative enzymes that synergistically and efficiently degrade lignin. The major groups of ligninolytic enzymes include lignin peroxidases, manganese peroxidases, versatile peroxidases, and laccases. The peroxidases are heme-containing enzymes with catalytic cycles that involve the activation by H2O2 and substrate reduction of compound I and compound II intermediates. Lignin peroxidases have the unique ability to catalyze oxidative cleavage of C-C bonds and ether (C-O-C) bonds in non-phenolic aromatic substrates of high redox potential. Manganese peroxidases oxidize Mn(II) to Mn(III), which facilitates the degradation of phenolic compounds or, in turn, oxidizes a second mediator for the breakdown of non-phenolic compounds. Versatile peroxidases are hybrids of lignin peroxidase and manganese peroxidase with a bifunctional characteristic. Laccases are multi-copper-containing proteins that catalyze the oxidation of phenolic substrates with concomitant reduction of molecular oxygen to water. This review covers the chemical nature of lignin substrates and focuses on the biochemical properties, molecular structures, reaction mechanisms, and related structures/functions of these enzymes.

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“…Fungal hyphae then sequester these lignin degradation products for internal catabolism. The enzyme is also highly active in the presence of organic solvents thereby effectively binding the inorganic cation manganese due to favourable decrease in medium polarity 21 . These aspects deliver versatile peroxidases as a novel biocatalyst for direct oxidation of a broad spectrum of aromatic heterogenic substrates, a feature significant for biotechnological applications of this enzyme.…”

Section: Catalytic Mechanism Of Versatile Peroxidasementioning

confidence: 99%

Insights into the Mechanism of Lignocellulose Degradation by Versatile Peroxidases

Ravichandran¹,

Sridhar²

2017

Current Science

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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.

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Catalytic activity of versatile peroxidase from Bjerkandera fumosa in aqueous solutions of water–miscible organic solvents

Cited by 33 publications

References 28 publications

Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system

Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system

Structure and Action Mechanism of Ligninolytic Enzymes

Insights into the Mechanism of Lignocellulose Degradation by Versatile Peroxidases

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