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      Biotechnology Potential of Marine Fungi Degrading Plant and Algae Polymeric Substrates

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          Abstract

          Filamentous fungi possess the metabolic capacity to degrade environment organic matter, much of which is the plant and algae material enriched with the cell wall carbohydrates and polyphenol complexes that frequently can be assimilated by only marine fungi. As the most renewable energy feedstock on the Earth, the plant or algae polymeric substrates induce an expression of microbial extracellular enzymes that catalyze their cleaving up to the component sugars. However, the question of what the marine fungi contributes to the plant and algae material biotransformation processes has yet to be highlighted sufficiently. In this review, we summarized the potential of marine fungi alternatively to terrestrial fungi to produce the biotechnologically valuable extracellular enzymes in response to the plant and macroalgae polymeric substrates as sources of carbon for their bioconversion used for industries and bioremediation.

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          Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes

          Background Since its inception, the carbohydrate-active enzymes database (CAZy; http://www.cazy.org) has described the families of enzymes that cleave or build complex carbohydrates, namely the glycoside hydrolases (GH), the polysaccharide lyases (PL), the carbohydrate esterases (CE), the glycosyltransferases (GT) and their appended non-catalytic carbohydrate-binding modules (CBM). The recent discovery that members of families CBM33 and family GH61 are in fact lytic polysaccharide monooxygenases (LPMO), demands a reclassification of these families into a suitable category. Results Because lignin is invariably found together with polysaccharides in the plant cell wall and because lignin fragments are likely to act in concert with (LPMO), we have decided to join the families of lignin degradation enzymes to the LPMO families and launch a new CAZy class that we name “Auxiliary Activities” in order to accommodate a range of enzyme mechanisms and substrates related to lignocellulose conversion. Comparative analyses of these auxiliary activities in 41 fungal genomes reveal a pertinent division of several fungal groups and subgroups combining their phylogenetic origin and their nutritional mode (white vs. brown rot). Conclusions The new class introduced in the CAZy database extends the traditional CAZy families, and provides a better coverage of the full extent of the lignocellulose breakdown machinery.
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            Laccases: a never-ending story.

            Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.
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              Fungal cellulases.

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                Author and article information

                Contributors
                Journal
                Front Microbiol
                Front Microbiol
                Front. Microbiol.
                Frontiers in Microbiology
                Frontiers Media S.A.
                1664-302X
                10 July 2018
                2018
                : 9
                : 1527
                Affiliations
                [1] 1G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences , Vladivostok, Russia
                [2] 2Innovative Technology Center, Far Eastern Federal University , Vladivostok, Russia
                Author notes

                Edited by: Raffaella Balestrini, Consiglio Nazionale delle Ricerche (CNR), Italy

                Reviewed by: Giovanna Cristina Varese, Università degli Studi di Torino, Italy; Diego Fabian Gomez-Casati, National University of Rosario, Argentina

                *Correspondence: Larissa Balabanova, balaban@ 123456piboc.dvo.ru

                This article was submitted to Fungi and Their Interactions, a section of the journal Frontiers in Microbiology

                Article
                10.3389/fmicb.2018.01527
                6052901
                30050513
                4c9c5eb4-7f20-4e67-9bf2-1424105d6843
                Copyright © 2018 Balabanova, Slepchenko, Son and Tekutyeva.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 15 March 2018
                : 19 June 2018
                Page count
                Figures: 1, Tables: 1, Equations: 0, References: 139, Pages: 15, Words: 0
                Funding
                Funded by: Ministry of Education and Science of the Russian Federation 10.13039/501100003443
                Award ID: Agreement 02.G25.31.0172, 01.12.2015
                Categories
                Microbiology
                Review

                Microbiology & Virology
                filamentous fungi,marine-derived fungi,glycoside hydrolases,algae polysaccharides,plant polysaccharide-degrading enzymes,lignocellulolytic enzymes

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