Oxidoreductases peroxidases

So far, several oxidoreductases, peroxidase, laccase, polyphenol oxidase (tyrosinase), and so on have been reported to catalyze oxidative polymerization of phenol derivatives among which peroxidase is most often used [165,166]. Peroxidase is an enzyme that catalyzes the oxidation of a donor to an oxidized donor by the action of hydrogen peroxide, liberating two water molecules. Horseradish peroxidase (HRP) is a single-chain p-type hemoprotein that catalyzes the decomposition of hydrogen peroxide at the expense of aromatic proton donors. 

Oxidoreductases are enzymes that catalyze the reversible transfer of hydrogen atoms and electrons from one molecule (the reductant) to another (the oxidant). During the last four decades, a variety of oxidoreductases (peroxidases, oxidases. 

Oxidoreductases Peroxidases Phenols, anUines, vinyl compounds... 

For the last decades, enzymatic synthesis of phenolic polymers has been extensively investigated [1-10]. In living cells, various oxidoreductases play an important role in maintaining the metabolism of living systems. So far, several oxidoreductases—peroxidase, laccase, bilirubin oxidase etc.—have been reported to catalyze an oxidative polymerization of phenol derivatives, and among them, peroxidase is most often used. The enzymatically synthesized phenolic polymers are expected to become an alternative to conventional phenolic resins, which have limitations of their preparation and use due to concerns over the toxicity of formaldehyde. 

Oxidoreductases Peroxidase, laccase, tyrosinase, glucose oxidase Polyphenols, polyanilines, vinyl polymers... 

Oxidoreductases dehydrogenase, oxidase oxygenase, peroxidase oxidation or reduction... 

Horseradish peroxidase (HRP) is a member of the large class of peroxidases, which are enzymes defined as oxidoreductases using hydroperoxide as electron acceptor. HRP has been widely used for the construction of amperometric biosensor for the determination of H202 and small organic and inorganic substrates. 

A broad spectrum of chemical reactions can be catalyzed by enzymes Hydrolysis, esterification, isomerization, addition and elimination, alkylation and dealkylation, halogenation and dehalogenation, and oxidation and reduction. The last reactions are catalyzed by redox enzymes, which are classified as oxidoreductases and divided into four categories according to the oxidant they utilize and the reactions they catalyze 1) dehydrogenases (reductases), 2) oxidases, 3) oxygenases (mono- and dioxygenases), and 4) peroxidases. The latter enzymes have received extensive attention in the last years as bio catalysts for synthetic applications. Peroxidases catalyze the oxidation of aromatic compounds, oxidation of heteroatom compounds, epoxidation, and the enantio-selective reduction of racemic hydroperoxides. In this article, a short overview... 

These findings led to the proposition that the veratryl alcohol is degraded via the quinone intermediates (Figure 5) to CO2 through a series of transformations involving lignin peroxidase, perhydroxy radicals and the NADP-dependent aryl alcohol oxidoreductase. Veratraldehyde, the major product of lignin peroxidase catalyzed veratryl alcohol oxidation, is rapidly reduced back to veratryl alcohol it is the further metabolism of the side products of the oxidative process, viz. the quinones and lactones, that drives the overall transformation towards completion (34). 

In the field of bioremediation, oxidoreductases are considered to be excellent biocatalysts for environmentally friendly processes. Laccases and peroxidases are widely used to treat effluents from pulp/cotton mills, food/fruit processing plants and breweries [1, 2, 37]. Laccases, peroxidases and other oxygenases are also being studied for their abihty to degrade hazardous coal substances, especially the sulfur-containing components, and in the treatment of industrial waste and contaminated soil and water in the transformation of xenobiotics, polycycHc aromatic hydrocarbons and other pollutants (biodetoxification and biodecontamination)... 

O2 oxidoreductase (E.C. 1.10.3.1.) and peroxidase (E.C. 1.11.1.7.) contribute to secondary pigment formation during curing processes (J ) and during stresses to plants caused by ozone ( > ) diseases, chemicals, physical wounding and adverse temperatures, moisture and nutrient levels (, ). The resulting pigments contribute to abnormal foliar and food coloration (6) and flavors (, 7) of plants and plant products. 

Mason (30) and Pierpoint (31) have described the involvement of o-diphenols in plants and how they contribute to abnormal plant pigmentation. o-Diphenols are oxidized to o-quinones by enzymes of the phenolase complex (o-diphenol O2 oxidoreductase, E.C. 1.10.3.1) and by peroxidase (E.C. 1.11.1.7). o-Quinones react with amino acids, proteins, amines and thiol groups of proteins to polymerize and from reddish-brown pigments. Concentrations of caffeic acid are doubled in both bean (8) and peanut... 

---