Abstract
Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth.
Highlights
Enzymes are biological catalysts that facilitate the conversion of substrates into products providing favorable conditions that lower the activation energy of the reaction [1]
According to Adewale and Adekunle [16], the peroxidases obtained from C. nitidia, the isoenzymes B of the red C. nitidia exhibited the best combination of properties that was found to be useful in biotechnological application
Over 99% biodegradation of high concentration of total petroleum hydrocarbons (TPH) was achieved in the H2O2-induced sequencing batch reactor (SBR) operated at a relatively short reaction time using a low dose of H2O2 [78]
Summary
Enzymes are biological catalysts that facilitate the conversion of substrates into products providing favorable conditions that lower the activation energy of the reaction [1] They play an important role as cost-effective and environmentally sensitive substituents for chemical processes in industries such as textile manufacturing, pharmaceutical, laundry, pulp and paper production [2,3]. Peroxidases are ubiquitous enzymes belonging to the class of oxidoreductase [4,6,7,8,9,10,11,12,13,14] They generally catalyze a variety of oxygen-transfer reactions between hydrogen peroxide or other peroxides as electron acceptors and many kinds of substrates (xenobiotics, lignin and other phenolic compounds) by means of oxygen (O2) liberation from H2O2 [6,14]. Lignin peroxidase (LiP) and MnP are both heme proteins, used in the hydrolysis of lignocellulosic agricultural residues for the degradation of complex and recalcitrant constituent lignin
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