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      Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment

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          Abstract

          Ligninolytic enzymes play a key role in degradation and detoxification of lignocellulosic waste in environment. The major ligninolytic enzymes are laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase. The activities of these enzymes are enhanced by various mediators as well as some other enzymes (feruloyl esterase, aryl-alcohol oxidase, quinone reductases, lipases, catechol 2, 3-dioxygenase) to facilitate the process for degradation and detoxification of lignocellulosic waste in environment. The structurally laccase is isoenzymes with monomeric or dimeric and glycosylation levels (10–45%). This contains four copper ions of three different types. The enzyme catalyzes the overall reaction: 4 benzenediol + O 2 to 4 benzosemiquinone + 2H 2O. While, lignin peroxidase is a glycoprotein molecular mass of 38–46 kDa containing one mole of iron protoporphyrin IX per one mol of protein, catalyzes the H 2O 2 dependent oxidative depolymerization of lignin. The manganese peroxidase is a glycosylated heme protein with molecular mass of 40–50kDa. It depolymerizes the lignin molecule in the presence of manganese ion. The versatile peroxidase has broad range substrate sharing typical features of the manganese and lignin peroxidase families. Although ligninolytic enzymes have broad range of industrial application specially the degradation and detoxification of lignocellulosic waste discharged from various industrial activities, its large scale application is still limited due to lack of limited production. Further, the extremophilic properties of ligninolytic enzymes indicated their broad prospects in varied environmental conditions. Therefore it needs more extensive research for understanding its structure and mechanisms for broad range commercial applications.

          Abstract

          Laccase; Lignin peroxidase; Manganese peroxidase; Versatile peroxidase; Lignocellulosic waste; Degradation and detoxification, Environmental science, Microbiology.

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          Lignocellulosic residues: biodegradation and bioconversion by fungi.

          The ability of fungi to degrade lignocellulosic materials is due to their highly efficient enzymatic system. Fungi have two types of extracellular enzymatic systems; the hydrolytic system, which produces hydrolases that are responsible for polysaccharide degradation and a unique oxidative and extracellular ligninolytic system, which degrades lignin and opens phenyl rings. Lignocellulosic residues from wood, grass, agricultural, forestry wastes and municipal solid wastes are particularly abundant in nature and have a potential for bioconversion. Accumulation of lignocellulosic materials in large quantities in places where agricultural residues present a disposal problem results not only in deterioration of the environment but also in loss of potentially valuable material that can be used in paper manufacture, biomass fuel production, composting, human and animal feed among others. Several novel markets for lignocellulosic residues have been identified recently. The use of fungi in low cost bioremediation projects might be attractive given their lignocellulose hydrolysis enzyme machinery.
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            Novel enzymes for the degradation of cellulose

            The bulk terrestrial biomass resource in a future bio-economy will be lignocellulosic biomass, which is recalcitrant and challenging to process. Enzymatic conversion of polysaccharides in the lignocellulosic biomass will be a key technology in future biorefineries and this technology is currently the subject of intensive research. We describe recent developments in enzyme technology for conversion of cellulose, the most abundant, homogeneous and recalcitrant polysaccharide in lignocellulosic biomass. In particular, we focus on a recently discovered new type of enzymes currently classified as CBM33 and GH61 that catalyze oxidative cleavage of polysaccharides. These enzymes promote the efficiency of classical hydrolytic enzymes (cellulases) by acting on the surfaces of the insoluble substrate, where they introduce chain breaks in the polysaccharide chains, without the need of first “extracting” these chains from their crystalline matrix.
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              Pathways for degradation of lignin in bacteria and fungi.

              Lignin is a heterogeneous aromatic polymer found as 10-35% of lignocellulose, found in plant cell walls. The bio-conversion of plant lignocellulose to glucose is an important part of second generation biofuel production, but the resistance of lignin to breakdown is a major obstacle in this process, hence there is considerable interest in the microbial breakdown of lignin. White-rot fungi are known to break down lignin with the aid of extracellular peroxidase and laccase enzymes. There are also reports of bacteria that can degrade lignin, and recent work indicates that bacterial lignin breakdown may be more significant than previously thought. The review will discuss the enzymes for lignin breakdown in fungi and bacteria, and the catabolic pathways for breakdown of the β-aryl ether, biphenyl and other components of lignin in bacteria and fungi. The review will also discuss small molecule phenolic breakdown products from lignin that have been identified from lignin-degrading microbes, and includes a bioinformatic analysis of the occurrence of known lignin-degradation pathways in Gram-positive and Gram-negative bacteria.
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                Author and article information

                Contributors
                Journal
                Heliyon
                Heliyon
                Heliyon
                Elsevier
                2405-8440
                19 February 2020
                February 2020
                19 February 2020
                : 6
                : 2
                : e03170
                Affiliations
                [1]Department of Environmental Microbiology, School for Environmental Sciences, Babasaheb Bhimrao Ambedkar (A Central) University, Vidya Vihar, Raebareli Road, Lucknow, Uttar Pradesh, 226025, India
                Author notes
                []Corresponding author. prof.chandrabbau@ 123456gmail.com
                Article
                S2405-8440(20)30015-3 e03170
                10.1016/j.heliyon.2020.e03170
                7033530
                32095645
                b6d77508-d2f2-4aa9-abe1-5d862b98ad9a
                © 2020 The Authors

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                : 6 July 2019
                : 4 October 2019
                : 31 December 2019
                Categories
                Article

                laccase,lignin peroxidase,manganese peroxidase,versatile peroxidase,lignocellulosic waste,degradation and detoxification,environmental science,microbiology

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