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Polysaccharide monooxygenase

Rebecca C Gregory, Glyn R Hemsworth, Johan P Turkenburg, Samuel J Hart, Paul H Walton, Gideon J Davies
The enzymatic deconstruction of recalcitrant polysaccharide biomass is central to the conversion of these substrates for societal benefit, such as in biofuels. Traditional models for enzyme-catalysed polysaccharide degradation involved the synergistic action of endo-, exo- and processive glycoside hydrolases working in concert to hydrolyse the substrate. More recently this model has been succeeded by one featuring a newly discovered class of mononuclear copper enzymes: lytic polysaccharide monooxygenases (LPMOs; classified as Auxiliary Activity (AA) enzymes in the CAZy classification)...
September 29, 2016: Dalton Transactions: An International Journal of Inorganic Chemistry
Mi-Ji Yu, Sun-Hee Yoon, Young-Wan Kim
Lytic polysaccharide monooxygenases (LPMOs) are copper ion-containing enzymes that degrade crystalline polysaccharides, such as cellulose or chitin, through an oxidative mechanism. To the best of our knowledge, there are no assay methods for the direct characterization of LPMOs that degrade substrates without coupled enzymes. As such, in this study, a coupled enzyme-free assay method for LPMOs was developed, which is based on measuring the consumption of ascorbic acid used as an external electron donor for LPMOs...
November 2016: Enzyme and Microbial Technology
Jennifer S M Loose, Zarah Forsberg, Daniel Kracher, Stefan Scheiblbrandner, Roland Ludwig, Vincent G H Eijsink, Gustav Vaaje-Kolstad
Lytic polysaccharide monooxygenases (LPMOs) represent a recent addition to the carbohydrate-active enzymes and are classified as auxiliary activity (AA) families 9, 10, 11 and 13. LPMOs are crucial for effective degradation of recalcitrant polysaccharides like cellulose or chitin. These enzymes are copper-dependent and utilize a redox mechanism to cleave glycosidic bonds that is dependent on molecular oxygen and an external electron donor. The electrons can be provided by various sources, such as chemical compounds (e...
September 19, 2016: Protein Science: a Publication of the Protein Society
Shingo Miyauchi, David Navarro, Igor V Grigoriev, Anna Lipzen, Robert Riley, Didier Chevret, Sacha Grisel, Jean-Guy Berrin, Bernard Henrissat, Marie-Noëlle Rosso
Wood-decay fungi contain the cellular mechanisms to decompose such plant cell wall components as cellulose, hemicellulose, and lignin. A multi-omics approach to the comparative analysis of wood-decay fungi gives not only new insights into their strategies for decomposing recalcitrant plant biomass, but also an understanding of how to exploit these mechanisms for biotechnological applications. We have developed an analytical workflow, Applied Biomass Conversion Design for Efficient Fungal Green Technology (ABCDEFGT), to simplify the analysis and interpretation of transcriptomic and secretomic data...
2016: Frontiers in Microbiology
Jaana Kuuskeri, Mari Häkkinen, Pia Laine, Olli-Pekka Smolander, Fitsum Tamene, Sini Miettinen, Paula Nousiainen, Marianna Kemell, Petri Auvinen, Taina Lundell
BACKGROUND: The white-rot Agaricomycetes species Phlebia radiata is an efficient wood-decaying fungus degrading all wood components, including cellulose, hemicellulose, and lignin. We cultivated P. radiata in solid state cultures on spruce wood, and extended the experiment to 6 weeks to gain more knowledge on the time-scale dynamics of protein expression upon growth and wood decay. Total proteome and transcriptome of P. radiata were analyzed by peptide LC-MS/MS and RNA sequencing at specific time points to study the enzymatic machinery on the fungus' natural growth substrate...
2016: Biotechnology for Biofuels
Gerdt Müller, Dayanand Chandrahas Kalyani, Svein Jarle Horn
Enzymatic catalysis plays a key role in the conversion of lignocellulosic biomass to fuels and chemicals such as lactic acid. In the last decade, the efficiency of commercial cellulase cocktails has increased significantly, in part due to the inclusion of lytic polysaccharide monooxygenases (LPMOs). However, the LPMOs' need for molecular oxygen to break down cellulose demands reinvestigations of process conditions. In this study, we evaluate the efficiency of lactic acid production from steam-exploded birch using an LPMO-containing cellulase cocktail in combination with lactic acid bacteria, investigating both separate hydrolysis and fermentation (SHF) and simultaneous saccharification and fermentation (SSF)...
September 6, 2016: Biotechnology and Bioengineering
Yuka Kojima, Anikó Várnai, Takuya Ishida, Naoki Sunagawa, Dejan M Petrovic, Kiyohiko Igarashi, Jody Jellison, Barry Goodell, Gry Alfredsen, Bjørge Westereng, Vincent G H Eijsink, Makoto Yoshida
: Fungi secrete a set of glycoside hydrolases and lytic polysaccharide monooxygenases (LPMOs) to degrade plant polysaccharides. Brown-rot fungi, such as Gloeophyllum trabeum, tend to have few LPMOs and information on these enzymes is scarce. The genome of G. trabeum encodes four AA9 LPMOs, whose coding sequences were amplified from cDNA. Due to alternative splicing, two variants of GtLPMO9A seem to be produced, a single domain variant, GtLPMO9A-1, and a longer variant, GtLPMO9A-2, which contains a C-terminal domain comprising approximately 55 residues without a predicted function...
September 2, 2016: Applied and Environmental Microbiology
Laura Nekiunaite, Magnus Ø Arntzen, Birte Svensson, Gustav Vaaje-Kolstad, Maher Abou Hachem
BACKGROUND: Starch is the second most abundant plant-derived biomass and a major feedstock in non-food industrial applications and first generation biofuel production. In contrast to lignocellulose, detailed insight into fungal degradation of starch is currently lacking. This study explores the secretomes of Aspergillus nidulans grown on cereal starches from wheat and high-amylose (HA) maize, as well as legume starch from pea for 5 days. RESULTS: Aspergillus nidulans grew efficiently on cereal starches, whereas growth on pea starch was poor...
2016: Biotechnology for Biofuels
Matthias Frommhagen, Martijn J Koetsier, Adrie H Westphal, Jaap Visser, Sandra W A Hinz, Jean-Paul Vincken, Willem J H van Berkel, Mirjam A Kabel, Harry Gruppen
BACKGROUND: Lytic polysaccharide monooxgygenases (LPMOs) are known to boost the hydrolytic breakdown of lignocellulosic biomass, especially cellulose, due to their oxidative mechanism. For their activity, LPMOs require an electron donor for reducing the divalent copper cofactor. LPMO activities are mainly investigated with ascorbic acid as a reducing agent, but little is known about the effect of plant-derived reducing agents on LPMOs activity. RESULTS: Here, we show that three LPMOs from the fungus Myceliophthora thermophila C1, MtLPMO9A, MtLPMO9B and MtLPMO9C, differ in their substrate preference, C1-/C4-regioselectivity and reducing agent specificity...
2016: Biotechnology for Biofuels
Katja Salomon Johansen
Lytic polysaccharide monooxygenases (LPMOs) are copper-enzymes that catalyze oxidative cleavage of glycosidic bonds. These enzymes are secreted by many microorganisms to initiate infection and degradation processes. In particular, the concept of fungal degradation of lignocellulose has been revised in the light of this recent finding. LPMOs require a source of electrons for activity, and both enzymatic and plant-derived sources have been identified. Importantly, light-induced electron delivery from light-harvesting pigments can efficiently drive LPMO activity...
August 12, 2016: Trends in Plant Science
Sona Garajova, Yann Mathieu, Maria Rosa Beccia, Chloé Bennati-Granier, Frédéric Biaso, Mathieu Fanuel, David Ropartz, Bruno Guigliarelli, Eric Record, Hélène Rogniaux, Bernard Henrissat, Jean-Guy Berrin
The enzymatic conversion of plant biomass has been recently revolutionized by the discovery of lytic polysaccharide monooxygenases (LPMOs) that carry out oxidative cleavage of polysaccharides. These very powerful enzymes are abundant in fungal saprotrophs. LPMOs require activation by electrons that can be provided by cellobiose dehydrogenases (CDHs), but as some fungi lack CDH-encoding genes, other recycling enzymes must exist. We investigated the ability of AA3_2 flavoenzymes secreted under lignocellulolytic conditions to trigger oxidative cellulose degradation by AA9 LPMOs...
2016: Scientific Reports
A G Bulakhov, A V Gusakov, A V Chekushina, A D Satrutdinov, A V Koshelev, V Yu Matys, A P Sinitsyn
Lytic polysaccharide monooxygenases (PMO) discovered several years ago are enzymes classified as oxidoreductases. In nature, they participate in microbial degradation of cellulose together with cellulases that belong to the hydrolytic type of enzymes (class of hydrolases). Three PMO from ascomycetes - Thielavia terrestris, Trichoderma reesei, and Myceliophthora thermophila - were isolated and purified to homogeneous state using various types of chromatography. The first two enzymes are recombinant proteins heterologously expressed by the Penicillium verruculosum fungus, while the third is a native PMO secreted by M...
May 2016: Biochemistry. Biokhimii︠a︡
Ilabahen Patel, Daniel Kracher, Su Ma, Sona Garajova, Mireille Haon, Craig B Faulds, Jean-Guy Berrin, Roland Ludwig, Eric Record
BACKGROUND: Lytic polysaccharide monooxygenases (LPMOs) belong to the "auxiliary activities (AA)" enzyme class of the CAZy database. They are known to strongly improve the saccharification process and boost soluble sugar yields from lignocellulosic biomass, which is a key step in the efficient production of sustainable economic biofuels. To date, most LPMOs have been characterized from terrestrial fungi, but novel fungal LPMOs isolated from more extreme environments such as an estuary mangrove ecosystem could offer enzymes with unique properties in terms of salt tolerance and higher stability under harsh condition...
2016: Biotechnology for Biofuels
Van V Vu, Michael A Marletta
Polysaccharide degradation by hydrolytic enzymes glycoside hydrolases (GHs) is well known. More recently, polysaccharide monooxygenases (PMOs, also known as lytic PMOs or LPMOs) were found to oxidatively degrade various polysaccharides via a copper-dependent hydroxylation. PMOs were previously thought to be either GHs or carbohydrate binding modules (CBMs), and have been re-classified in carbohydrate active enzymes (CAZY) database as auxiliary activity (AA) families. These enzymes include cellulose-active fungal PMOs (AA9, formerly GH61), chitin- and cellulose-active bacterial PMOs (AA10, formerly CBM33), and chitin-active fungal PMOs (AA11)...
July 2016: Cellular and Molecular Life Sciences: CMLS
Tina Rise Tuveng, Magnus Øverlie Arntzen, Oskar Bengtsson, Jeffrey G Gardner, Gustav Vaaje-Kolstad, Vincent G H Eijsink
Studies of the secretomes of microbes grown on insoluble substrates are important for the discovery of novel proteins involved in biomass conversion. However, data in literature and this study indicate that secretome samples tend to be contaminated with cytoplasmic proteins. We have examined the secretome of the Gram-negative soil bacterium Cellvibrio japonicus using a simple plate-based culturing technique that yields samples with high fractions (60-75%) of proteins that are predicted to be secreted. By combining this approach with label-free quantification using the MaxLFQ algorithm, we have mapped and quantified proteins secreted by C...
July 2016: Proteomics
Gaston Courtade, Reinhard Wimmer, Åsmund K Røhr, Marita Preims, Alfons K G Felice, Maria Dimarogona, Gustav Vaaje-Kolstad, Morten Sørlie, Mats Sandgren, Roland Ludwig, Vincent G H Eijsink, Finn Lillelund Aachmann
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds using molecular oxygen and an external electron donor. We have used NMR and isothermal titration calorimetry (ITC) to study the interactions of a broad-specificity fungal LPMO, NcLPMO9C, with various substrates and with cellobiose dehydrogenase (CDH), a known natural supplier of electrons. The NMR studies revealed interactions with cellohexaose that center around the copper site. NMR studies with xyloglucans, i...
May 24, 2016: Proceedings of the National Academy of Sciences of the United States of America
Gaston Courtade, Reinhard Wimmer, Maria Dimarogona, Mats Sandgren, Vincent G H Eijsink, Finn L Aachmann
The apo-form of the 23.3 kDa catalytic domain of the AA9 family lytic polysaccharide monooxygenase NcLPMO9C from Neurospora crassa has been isotopically labeled and recombinantly expressed in Pichia pastoris. In this paper, we report the (1)H, (13)C, and (15)N chemical shift assignments of this LPMO.
October 2016: Biomolecular NMR Assignments
Amanda K Chaplin, Michael T Wilson, Michael A Hough, Dimitri A Svistunenko, Glyn R Hemsworth, Paul H Walton, Erik Vijgenboom, Jonathan A R Worrall
Copper-dependent lytic polysaccharide monooxygenases (LPMOs) are enzymes that oxidatively deconstruct polysaccharides. The active site copper in LPMOs is coordinated by a histidine-brace. This utilizes the amino group and side chain of the N-terminal His residue with the side chain of a second His residue to create a T-shaped arrangement of nitrogen ligands. We report a structural, kinetic, and thermodynamic appraisal of copper binding to the histidine-brace in an auxiliary activity family 10 (AA10) LPMO from Streptomyces lividans (SliLPMO10E)...
June 10, 2016: Journal of Biological Chemistry
Daniel Kracher, Stefan Scheiblbrandner, Alfons K G Felice, Erik Breslmayr, Marita Preims, Karolina Ludwicka, Dietmar Haltrich, Vincent G H Eijsink, Roland Ludwig
Ninety percent of lignocellulose-degrading fungi contain genes encoding lytic polysaccharide monooxygenases (LPMOs). These enzymes catalyze the initial oxidative cleavage of recalcitrant polysaccharides after activation by an electron donor. Understanding the source of electrons is fundamental to fungal physiology and will also help with the exploitation of LPMOs for biomass processing. Using genome data and biochemical methods, we characterized and compared different extracellular electron sources for LPMOs: cellobiose dehydrogenase, phenols procured from plant biomass or produced by fungi, and glucose-methanol-choline oxidoreductases that regenerate LPMO-reducing diphenols...
May 27, 2016: Science
Paul H Walton, Gideon J Davies
Lytic polysaccharide monooxygenases (LPMOs) are recently discovered copper-containing oxygenases. LPMOs oxidise recalcitrant polysaccharides such as chitin and cellulose, thereby making these substrates more tractable to canonical chitinase or cellulase action. As such, LPMOs are attracting much attention not only for their capacity to greatly increase the efficiency of production of cellulosic-based biofuels, but also for the new questions they pose about the mechanisms of biological oxidation of recalcitrant substrates...
April 2016: Current Opinion in Chemical Biology
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