Lignin is a class of complex organic polymers that form key structural materials in the support tissues of most plants. Lignins are particularly important in the formation of cell walls, especially in wood and bark, because they lend rigidity and do not rot easily. Chemically, lignins are polymers made by cross-linking phenolic precursors.
The Polyporales are an order of about 1800 species of fungi in the division Basidiomycota. The order includes some polypores as well as many corticioid fungi and a few agarics. Many species within the order are saprotrophic, most of them wood-rotters. Some genera, such as Ganoderma and Fomes, contain species that attack living tissues and then continue to degrade the wood of their dead hosts. Those of economic importance include several important pathogens of trees and a few species that cause damage by rotting structural timber. Some of the Polyporales are commercially cultivated and marketed for use as food items or in traditional Chinese medicine.
Mycoremediation is a form of bioremediation in which fungi-based remediation methods are used to decontaminate the environment. Fungi have been proven to be a cheap, effective and environmentally sound way for removing a wide array of contaminants from damaged environments or wastewater. These contaminants include heavy metals, organic pollutants, textile dyes, leather tanning chemicals and wastewater, petroleum fuels, polycyclic aromatic hydrocarbons, pharmaceuticals and personal care products, pesticides and herbicides in land, fresh water, and marine environments.
Pleurotus eryngii is an edible mushroom native to Mediterranean regions of Europe, the Middle East, and North Africa, but also grown in many parts of Asia.
Pleurotus is a genus of gilled mushrooms which includes one of the most widely eaten mushrooms, P. ostreatus. Species of Pleurotus may be called oyster, abalone, or tree mushrooms, and are some of the most commonly cultivated edible mushrooms in the world. Pleurotus fungi have also been used in mycoremediation of pollutants, such as petroleum and polycyclic aromatic hydrocarbons.
Ascorbate peroxidase (or L-ascorbate peroxidase, APX) (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction
Laccases are multicopper oxidases found in plants, fungi, and bacteria. Laccases oxidize a variety of phenolic substrates, performing one-electron oxidations, leading to crosslinking. For example, laccases play a role in the formation of lignin by promoting the oxidative coupling of monolignols, a family of naturally occurring phenols. Other laccases, such as those produced by the fungus Pleurotus ostreatus, play a role in the degradation of lignin, and can therefore be classed as lignin-modifying enzymes. Other laccases produced by fungi can facilitate the biosynthesis of melanin pigments. Laccases catalyze ring cleavage of aromatic compounds.
Lignin-modifying enzymes (LMEs) are various types of enzymes produced by fungi and bacteria that catalyze the breakdown of lignin, a biopolymer commonly found in the cell walls of plants. The terms ligninases and lignases are older names for the same class, but the name "lignin-modifying enzymes" is now preferred, given that these enzymes are not hydrolytic but rather oxidative by their enzymatic mechanisms. LMEs include peroxidases, such as lignin peroxidase, manganese peroxidase, versatile peroxidase, and many phenoloxidases of the laccase type.
A wood-decay or xylophagous fungus is any species of fungus that digests moist wood, causing it to rot. Some species of wood-decay fungi attack dead wood, such as brown rot, and some, such as Armillaria, are parasitic and colonize living trees. Excessive moisture above the fibre saturation point in wood is required for fungal colonization and proliferation. In nature, this process causes the breakdown of complex molecules and leads to the return of nutrients to the soil. Wood-decay fungi consume wood in various ways; for example, some attack the carbohydrates in wood, and some others decay lignin. The rate of decay of wooden materials in various climates can be estimated by empirical models.
Bjerkandera adusta, commonly known as the smoky polypore or smoky bracket, is a species of fungus in the family Meruliaceae. It is a plant pathogen that causes white rot in live trees, but most commonly appears on dead wood. It was first described scientifically as Boletus adustus by Carl Ludwig Willdenow in 1787. The genome sequence of Bjerkandera adusta was reported in 2013. The species is inedible.
In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a manganese peroxidase (EC 1.11.1.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction
The ascorbate-glutathione cycle, sometimes Foyer-Halliwell-Asada pathway, is a metabolic pathway that detoxifies hydrogen peroxide (H2O2), a reactive oxygen species that is produced as a waste product in metabolism. The cycle involves the antioxidant metabolites: ascorbate, glutathione and NADPH and the enzymes linking these metabolites.
Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
Dye-decolorizing peroxidase (EC 1.11.1.19, DyP, DyP-type peroxidase) is an enzyme with systematic name Reactive-Blue-5:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction
Unspecific peroxygenase (EC 1.11.2.1, aromatic peroxygenase, mushroom peroxygenase, haloperoxidase-peroxygenase, Agrocybe aegerita peroxidase) is an enzyme with systematic name substrate:hydrogen peroxide oxidoreductase (RH-hydroxylating or -epoxidising). This enzyme catalyses the following chemical reaction
Extracellular enzymes or exoenzymes are synthesized inside the cell and then secreted outside the cell, where their function is to break down complex macromolecules into smaller units to be taken up by the cell for growth and assimilation. These enzymes degrade complex organic matter such as cellulose and hemicellulose into simple sugars that enzyme-producing organisms use as a source of carbon, energy, and nutrients. Grouped as hydrolases, lyases, oxidoreductases and transferases, these extracellular enzymes control soil enzyme activity through efficient degradation of biopolymers.
Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues.
Hypsizygus ulmarius, also known as the elm oyster mushroom, and less commonly as the elm leech, elm Pleurotus, is an edible fungus. It has often been confused with oyster mushrooms in the Pleurotus genus but can be differentiated easily as the gills are either not decurrent or not deeply decurrent. While not quite as common as true oyster mushrooms, they have a wide range globally in temperate forests. The mushrooms and vegetative hyphae of this species have been studied in recent years for their potential benefits to human health, and mycoremediation.
