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Polysaccharide monooxygenase

Bastien Bissaro, Ingvild Isaksen, Gustav Vaaje-Kolstad, Vincent G H Eijsink, Åsmund K Røhr
Lytic polysaccharide monooxygenases (LPMOs) are major players in biomass conversion, both in Nature and in the biorefining industry. How the mono-copper LPMO active site is positioned relative to the crystalline substrate surface to catalyze powerful, but potentially self-destructive, oxidative chemistry is one of the major questions in the field. We have adopted a multi-disciplinary approach, combining biochemical, spectroscopic and molecular modeling methods to study chitin binding by the well-studied LPMO from Serratia marcescens SmAA10A (or CBP21)...
March 2, 2018: Biochemistry
Federico Sabbadin, Glyn R Hemsworth, Luisa Ciano, Bernard Henrissat, Paul Dupree, Theodora Tryfona, Rita D S Marques, Sean T Sweeney, Katrin Besser, Luisa Elias, Giovanna Pesante, Yi Li, Adam A Dowle, Rachel Bates, Leonardo D Gomez, Rachael Simister, Gideon J Davies, Paul H Walton, Neil C Bruce, Simon J McQueen-Mason
Thermobia domestica belongs to an ancient group of insects and has a remarkable ability to digest crystalline cellulose without microbial assistance. By investigating the digestive proteome of Thermobia, we have identified over 20 members of an uncharacterized family of lytic polysaccharide monooxygenases (LPMOs). We show that this LPMO family spans across several clades of the Tree of Life, is of ancient origin, and was recruited by early arthropods with possible roles in remodeling endogenous chitin scaffolds during development and metamorphosis...
February 22, 2018: Nature Communications
Bo Song, Bingyao Li, Xiaoyan Wang, Wei Shen, Sungjin Park, Cynthia Collings, Anran Feng, Steve J Smith, Jonathan D Walton, Shi-You Ding
Background: The high cost of enzymes is one of the key technical barriers that must be overcome to realize the economical production of biofuels and biomaterials from biomass. Supplementation of enzyme cocktails with lytic polysaccharide monooxygenase (LPMO) can increase the efficiency of these cellulase mixtures for biomass conversion. The previous studies have revealed that LPMOs cleave polysaccharide chains by oxidization of the C1 and/or C4 carbons of the monomeric units. However, how LPMOs enhance enzymatic degradation of lignocellulose is still poorly understood...
2018: Biotechnology for Biofuels
Lukas Reisky, Hanna C Büchsenschütz, Jennifer Engel, Tao Song, Thomas Schweder, Jan-Hendrik Hehemann, Uwe T Bornscheuer
Sugar O-methylation shields algal polysaccharides against microbial hydrolytic enzymes. Here, we describe cytochrome P450 monooxygenases from marine bacteria that, together with appropriate redox-partner proteins, catalyze the oxidative demethylation of 6-O-methyl-D-galactose, which is an abundant monosaccharide of the algal polysaccharides agarose and porphyran. This previously unknown biological function extends the group of carbohydrate-active enzymes to include the class of cytochrome P450 monooxygenases...
February 19, 2018: Nature Chemical Biology
Jinguang Hu, Dong Tian, Scott Renneckar, Jack N Saddler
Physiochemical methods have generally been used to "open-up" biomass substrates/pulps and have been the main method used to fibrillate cellulose. However, recent work has shown that canonical cellulase enzymes such as endoglucanases, in combination with "amorphogenesis inducing" proteins such as lytic polysaccharide monooxygenases (LPMO), swollenin and hemicellulases, are able to increase cellulose accessibility. In the work reported here different combinations of endoglucanase, LPMO and xylanase were applied to Kraft pulps to assess their potential to induce fibrillation at low enzyme loading over a short time period...
February 16, 2018: Scientific Reports
Xiaobao Sun, Jiaxin Wan, Jiawen Cao, Yuexiu Si, Qian Wang
Lignocellulose is the most abundant renewable biomass resource. Enzymatic breakdown of lignocellulose into oligosaccharides or monosaccharides is the key to exploit lignocellulosic biomass. However, traditional glycoside hydrolases are insufficient to degrade lignocellulose. The emergence of lytic polysaccharide monooxygenase, a novel enzyme for lignocellulose degradation, has enriched the deconstruction schema and accelerated the enzymatic conversion of polysaccharides, by introducing new chain breaks that allow hydrolases to initiate further degradation...
February 25, 2018: Sheng Wu Gong Cheng Xue Bao, Chinese Journal of Biotechnology
Marie Couturier, Simon Ladevèze, Gerlind Sulzenbacher, Luisa Ciano, Mathieu Fanuel, Céline Moreau, Ana Villares, Bernard Cathala, Florence Chaspoul, Kristian E Frandsen, Aurore Labourel, Isabelle Herpoël-Gimbert, Sacha Grisel, Mireille Haon, Nicolas Lenfant, Hélène Rogniaux, David Ropartz, Gideon J Davies, Marie-Noëlle Rosso, Paul H Walton, Bernard Henrissat, Jean-Guy Berrin
Wood biomass is the most abundant feedstock envisioned for the development of modern biorefineries. However, the cost-effective conversion of this form of biomass into commodity products is limited by its resistance to enzymatic degradation. Here we describe a new family of fungal lytic polysaccharide monooxygenases (LPMOs) prevalent among white-rot and brown-rot basidiomycetes that is active on xylans-a recalcitrant polysaccharide abundant in wood biomass. Two AA14 LPMO members from the white-rot fungus Pycnoporus coccineus substantially increase the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers...
January 29, 2018: Nature Chemical Biology
Annette M Bodenheimer, William B O'Dell, Ryan C Oliver, Shuo Qian, Christopher B Stanley, Flora Meilleur
BACKGROUND: Cellobiose dehydrogenases have gained interest due to their potential applications in sectors from biofuel production to biomedical devices. The CDHIIA variant is comprised of a cytochrome domain (CYT), a dehydrogenase domain (DH), and a carbohydrate-binding module (CBM) that are connected by two flexible linkers. Upon cellobiose oxidation at the DH, intramolecular electron transfer (IaET) occurs from the DH to the CYT. In vivo, CDHIIA CYT subsequently performs intermolecular electron transfer (IeET) to a lytic polysaccharide monooxygenase (LPMO)...
January 25, 2018: Biochimica et Biophysica Acta
Lívia Brenelli, Fabio M Squina, Claus Felby, David Cannella
Background: The discovery of lignin as activator for the redox enzyme lytic polysaccharide monooxygenases (LPMOs) for the oxidation of cell-wall polysaccharides opens a new scenario for investigation of the interplay between different lignocellulose-degrading enzymes. The lignin-active enzymes in one hand, and the carbohydrate active in the other, are linked through a variety of electrons carrier molecules either derived from lignin or enzymatically transferred. Likewise, in nature, many lignocellulose-degrading organisms are expressing those enzymes simultaneously, and we wanted to test if a major commercial available lignin oxidase enzyme, i...
2018: Biotechnology for Biofuels
Brigitte Chabbert, Anouck Habrant, Mickaël Herbaut, Laurence Foulon, Véronique Aguié-Béghin, Sona Garajova, Sacha Grisel, Chloé Bennati-Granier, Isabelle Gimbert-Herpoël, Frédéric Jamme, Matthieu Réfrégiers, Christophe Sandt, Jean-Guy Berrin, Gabriel Paës
Lignocellulosic biomass bioconversion is hampered by the structural and chemical complexity of the network created by cellulose, hemicellulose and lignin. Biological conversion of lignocellulose involves synergistic action of a large array of enzymes including the recently discovered lytic polysaccharide monooxygenases (LPMOs) that perform oxidative cleavage of cellulose. Using in situ imaging by synchrotron UV fluorescence, we have shown that the addition of AA9 LPMO (from Podospora anserina) to cellulases cocktail improves the progression of enzymes in delignified Miscanthus x giganteus as observed at tissular levels...
December 19, 2017: Scientific Reports
Daniel Kracher, Martina Andlar, Paul G Furtmüller, Roland Ludwig
Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-containing enzymes that oxidatively degrade insoluble plant polysaccharides and soluble oligosaccharides. Upon reductive activation, they cleave the substrate and promote biomass degradation by hydrolytic enzymes. In this study we employed LPMO9C from Neurospora crassa, which is active towards cellulose and soluble β-glucans, to study the enzyme-substrate interaction and thermal stability. Binding studies showed that the reduction of the mononuclear active-site copper by ascorbic acid increased the affinity and the maximum binding capacity of LPMO for cellulose...
December 19, 2017: Journal of Biological Chemistry
Zhong-Peng Guo, Sophie Duquesne, Sophie Bozonnet, Jean-Marc Nicaud, Alain Marty, Michael Joseph O'Donohue
Background: A recently constructed cellulolytic Yarrowia lipolytica is able to grow efficiently on an industrial organosolv cellulose pulp, but shows limited ability to degrade crystalline cellulose. In this work, we have further engineered this strain, adding accessory proteins xylanase II (XYNII), lytic polysaccharide monooxygenase (LPMO), and swollenin (SWO) from Trichoderma reesei in order to enhance the degradation of recalcitrant substrate. Results: The production of EG I was enhanced using a promoter engineering strategy...
2017: Biotechnology for Biofuels
Luca Bertini, Raffaella Breglia, Matteo Lambrughi, Piercarlo Fantucci, Luca De Gioia, Marco Borsari, Marco Sola, Carlo Augusto Bortolotti, Maurizio Bruschi
Lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes that facilitate the degradation of recalcitrant polysaccharides by the oxidative cleavage of glycosidic bonds. They are gaining rapidly increasing attention as key players in biomass conversion, especially for the production of second-generation biofuels. Elucidation of the detailed mechanism of the LPMO reaction is a major step toward the assessment and optimization of LPMO efficacy in industrial biotechnology, paving the way to utilization of sustainable fuel sources...
January 2, 2018: Inorganic Chemistry
Richard A Owen, Paul K Fyfe, Adam Lodge, Jacob Biboy, Waldemar Vollmer, William N Hunter, Frank Sargent
The Gram-negative bacterium Serratia marcescens secretes many proteins that are involved in extracellular chitin degradation. This so-called chitinolytic machinery includes three types of chitinase enzymes and a lytic polysaccharide monooxygenase. An operon has been identified in S. marcescens , chiWXYZ , that is thought to be involved in the secretion of the chitinolytic machinery. Genetic evidence points to the ChiX protein being a key player in the secretion mechanism, since deletion of the chiX gene in S...
January 23, 2018: Biochemical Journal
Bing Liu, Åke Olson, Miao Wu, Anders Broberg, Mats Sandgren
Lytic polysaccharide monooxygenases (LPMO) are important redox enzymes produced by microorganisms for the degradation of recalcitrant natural polysaccharides. Heterobasidion irregulare is a white-rot phytopathogenic fungus that causes wood decay in conifers. The genome of this fungus encodes 10 putative Auxiliary Activity family 9 (AA9) LPMOs. We describe the first biochemical characterization of H. irregulare LPMOs through heterologous expression of two CBM-containing LPMOs from this fungus (HiLPMO9H, HiLPMO9I) in Pichia pastoris...
2017: PloS One
Zarah Forsberg, Bastien Bissaro, Jonathan Gullesen, Bjørn Dalhus, Gustav Vaaje-Kolstad, Vincent G H Eijsink
Bacterial lytic polysaccharide monooxygenases (LPMO10s) use redox chemistry to cleave glycosidic bonds in the two foremost recalcitrant polysaccharides found in nature, namely cellulose and chitin. Analysis of correlated mutations revealed that the substrate-binding and copper-containing surface of LPMO10s composes a network of co-evolved residues and interactions, whose roles in LPMO functionality are unclear. Here, we mutated a subset of these correlated residues in a newly characterized C1/C4-oxidizing LPMO10 from Micromonospora aurantiaca ( Ma LPMO10B) to the corresponding residues in strictly C1-oxidizing LPMO10s...
January 26, 2018: Journal of Biological Chemistry
Nathan Kruer-Zerhusen, Markus Alahuhta, Vladimir V Lunin, Michael E Himmel, Yannick J Bomble, David B Wilson
Background: Auxiliary activity (AA) enzymes are produced by numerous bacterial and fungal species to assist in the degradation of biomass. These enzymes are abundant but have yet to be fully characterized. Here, we report the X-ray structure of Thermobifida fusca AA10A (TfAA10A), investigate mutational characterization of key surface residues near its active site, and explore the importance of the various domains of Thermobifida fusca AA10B (TfAA10B). The structure of TfAA10A is similar to other bacterial LPMOs (lytic polysaccharide monooxygenases), including signs of photo-reduction and a distorted active site, with mixed features showing both type I and II copper coordination...
2017: Biotechnology for Biofuels
Matthias Frommhagen, Adrie H Westphal, Roelant Hilgers, Martijn J Koetsier, Sandra W A Hinz, Jaap Visser, Harry Gruppen, Willem J H van Berkel, Mirjam A Kabel
Lytic polysaccharide monooxygenases (LPMOs) have recently been shown to significantly enhance the degradation of recalcitrant polysaccharides and are of interest for the production of biochemicals and bioethanol from plant biomass. The copper-containing LPMOs utilize electrons, provided by reducing agents, to oxidatively cleave polysaccharides. Here, we report the development of a β-glucosidase-assisted method to quantify the release of C1-oxidized gluco-oligosaccharides from cellulose by two C1-oxidizing LPMOs from Myceliophthora thermophila C1...
February 2018: Applied Microbiology and Biotechnology
Silvia Hüttner, Thanh Thuy Nguyen, Zoraide Granchi, Thomas Chin-A-Woeng, Dag Ahrén, Johan Larsbrink, Vu Nguyen Thanh, Lisbeth Olsson
Background: Genome and transcriptome sequencing has greatly facilitated the understanding of biomass-degrading mechanisms in a number of fungal species. The information obtained enables the investigation and discovery of genes encoding proteins involved in plant cell wall degradation, which are crucial for saccharification of lignocellulosic biomass in second-generation biorefinery applications. The thermophilic fungus Malbranchea cinnamomea is an efficient producer of many industrially relevant enzymes and a detailed analysis of its genomic content will considerably enhance our understanding of its lignocellulolytic system and promote the discovery of novel proteins...
2017: Biotechnology for Biofuels
Raúl Castanera, Gúmer Pérez, Leticia López-Varas, Joëlle Amselem, Kurt LaButti, Vasanth Singan, Anna Lipzen, Sajeet Haridas, Kerrie Barry, Igor V Grigoriev, Antonio G Pisabarro, Lucía Ramírez
BACKGROUND: Coniophora olivacea is a basidiomycete fungus belonging to the order Boletales that produces brown-rot decay on dead wood of conifers. The Boletales order comprises a diverse group of species including saprotrophs and ectomycorrhizal fungi that show important differences in genome size. RESULTS: In this study we report the 39.07-megabase (Mb) draft genome assembly and annotation of C. olivacea. A total of 14,928 genes were annotated, including 470 putatively secreted proteins enriched in functions involved in lignocellulose degradation...
November 16, 2017: BMC Genomics
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