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Polysaccharide monooxygenase

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https://www.readbyqxmd.com/read/29259205/action-of-lytic-polysaccharide-monooxygenase-on-plant-tissue-is-governed-by-cellular-type
#1
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
https://www.readbyqxmd.com/read/29259126/active-site-copper-reduction-promotes-substrate-binding-of-fungal-lytic-polysaccharide-monooxygenase-and-reduces-stability
#2
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
https://www.readbyqxmd.com/read/29238402/expressing-accessory-proteins-in-cellulolytic-yarrowia-lipolytica-to-improve-the-conversion-yield-of-recalcitrant-cellulose
#3
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
https://www.readbyqxmd.com/read/29232119/catalytic-mechanism-of-fungal-lytic-polysaccharide-monooxygenases-investigated-by-first-principles-calculations
#4
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...
December 12, 2017: Inorganic Chemistry
https://www.readbyqxmd.com/read/29229757/structure-and-activity-of-chix-a-peptidoglycan-hydrolase-required-for-chitinase-secretion-by-serratia-marcescens
#5
Richard A Owen, Paul K Fyfe, Adam Lodge, Jacob Biboy, Waldemar Vollmer, William N Hunter, Frank Sargent
The Gram-negative bacterium Serratia marcescens secretes a number of 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...
December 11, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/29228039/biochemical-studies-of-two-lytic-polysaccharide-monooxygenases-from-the-white-rot-fungus-heterobasidion-irregulare-and-their-roles-in-lignocellulose-degradation
#6
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
https://www.readbyqxmd.com/read/29222333/structural-determinants-of-bacterial-lytic-polysaccharide-monooxygenase-functionality
#7
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 comprises a network of coevolved 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 (MaLPMO10B) to the corresponding residues in strictly C1-oxidizing LPMO10s...
December 8, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29213309/structure-of-a-thermobifida-fusca-lytic-polysaccharide-monooxygenase-and-mutagenesis-of-key-residues
#8
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
https://www.readbyqxmd.com/read/29196788/quantification-of-the-catalytic-performance-of-c1-cellulose-specific-lytic-polysaccharide-monooxygenases
#9
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...
December 2, 2017: Applied Microbiology and Biotechnology
https://www.readbyqxmd.com/read/29158777/combined-genome-and-transcriptome-sequencing-to-investigate-the-plant-cell-wall-degrading-enzyme-system-in-the-thermophilic-fungus-malbranchea-cinnamomea
#10
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
https://www.readbyqxmd.com/read/29145801/comparative-genomics-of-coniophora-olivacea-reveals-different-patterns-of-genome-expansion-in-boletales
#11
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
https://www.readbyqxmd.com/read/29138240/kinetics-of-h2o2-driven-degradation-of-chitin-by-a-bacterial-lytic-polysaccharide-monooxygenase
#12
Silja Kuusk, Bastien Bissaro, Piret Kuusk, Zarah Forsberg, Vincent G H Eijsink, Morten Sørlie, Priit Väljamäe
Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidative cleavage of glycosidic bonds in recalcitrant polysaccharides, such as cellulose and chitin, and are of interest in biotechnological utilization of these abundant biomaterials. It has recently been shown that LPMOs can use H2O2, instead of O2, as a co-substrate. This peroxygenase-like reaction by a mono-copper enzyme is unprecedented in nature and opens new avenues in chemistry and enzymology. Here, we provide the first detailed kinetic characterization of chitin degradation by the bacterial LPMO chitin-binding protein CBP21 using H2O2 as co-substrate...
November 14, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29100178/monitoring-of-reactions-catalyzed-by-lytic-polysaccharide-monooxygenases-using-highly-sensitive-fluorimetric-assay-of-the-oxygen-consumption-rate
#13
Alexander V Gusakov, Alexander G Bulakhov, Ilya N Demin, Arkady P Sinitsyn
Lytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that catalyze the oxidative deconstruction of polysaccharides. However fast and reliable methods of determination of LPMO activity still need to be developed, especially those based on the initial reaction rates. A method based on the oxygen consumption rate (OCR) measurements, using a Seahorse XFp Analyzer with highly-sensitive fluorimetric sensors, was applied for monitoring the oxidation of amorphous cellulose by three fungal LPMOs: recombinant enzymes from Thielavia terrestris (GH61E), Trichoderma reesei (Cel61A), and a native LPMO9A from Myceliophthora thermophila...
November 27, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/29100023/lignocellulose-deconstruction-in-the-biosphere
#14
REVIEW
Yannick J Bomble, Chien-Yuan Lin, Antonella Amore, Hui Wei, Evert K Holwerda, Peter N Ciesielski, Bryon S Donohoe, Stephen R Decker, Lee R Lynd, Michael E Himmel
Microorganisms have evolved different and yet complementary mechanisms to degrade biomass in the biosphere. The chemical biology of lignocellulose deconstruction is a complex and intricate process that appears to vary in response to specific ecosystems. These microorganisms rely on simple to complex arrangements of glycoside hydrolases to conduct most of these polysaccharide depolymerization reactions and also, as discovered more recently, oxidative mechanisms via lytic polysaccharide monooxygenases or non-enzymatic Fenton reactions which are used to enhance deconstruction...
October 31, 2017: Current Opinion in Chemical Biology
https://www.readbyqxmd.com/read/29057953/structural-and-electronic-determinants-of-lytic-polysaccharide-monooxygenase-reactivity-on-polysaccharide-substrates
#15
T J Simmons, K E H Frandsen, L Ciano, T Tryfona, N Lenfant, J C Poulsen, L F L Wilson, T Tandrup, M Tovborg, K Schnorr, K S Johansen, B Henrissat, P H Walton, L Lo Leggio, P Dupree
Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a functional and structural characterization of two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) and Collariella virescens (CvAA9A). LsAA9A and CvAA9A cleave a range of polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan and glucomannan. LsAA9A additionally cleaves isolated xylan substrates. The structures of CvAA9A and of LsAA9A bound to cellulosic and non-cellulosic oligosaccharides provide insight into the molecular determinants of their specificity...
October 20, 2017: Nature Communications
https://www.readbyqxmd.com/read/29026070/single-molecule-study-of-oxidative-enzymatic-deconstruction-of-cellulose
#16
Manuel Eibinger, Jürgen Sattelkow, Thomas Ganner, Harald Plank, Bernd Nidetzky
LPMO (lytic polysaccharide monooxygenase) represents a unique paradigm of cellulosic biomass degradation by an oxidative mechanism. Understanding the role of LPMO in deconstructing crystalline cellulose is fundamental to the enzyme's biological function and will help to specify the use of LPMO in biorefinery applications. Here we show with real-time atomic force microscopy that C1 and C4 oxidizing types of LPMO from Neurospora crassa (NcLPMO9F, NcLPMO9C) bind to nanocrystalline cellulose with high preference for the very same substrate surfaces that are also used by a processive cellulase (Trichoderma reesei CBH I) to move along during hydrolytic cellulose degradation...
October 12, 2017: Nature Communications
https://www.readbyqxmd.com/read/28919928/the-yeast-geotrichum-candidum-encodes-functional-lytic-polysaccharide-monooxygenases
#17
Simon Ladevèze, Mireille Haon, Ana Villares, Bernard Cathala, Sacha Grisel, Isabelle Herpoël-Gimbert, Bernard Henrissat, Jean-Guy Berrin
BACKGROUND: Lytic polysaccharide monooxygenases (LPMOs) are a class of powerful oxidative enzymes that have revolutionized our understanding of lignocellulose degradation. Fungal LPMOs of the AA9 family target cellulose and hemicelluloses. AA9 LPMO-coding genes have been identified across a wide range of fungal saprotrophs (Ascomycotina, Basidiomycotina, etc.), but so far they have not been found in more basal lineages. Recent genome analysis of the yeast Geotrichum candidum (Saccharomycotina) revealed the presence of several LPMO genes, which belong to the AA9 family...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28900033/high-resolution-structure-of-a-lytic-polysaccharide-monooxygenase-from-hypocrea-jecorina-reveals-a-predicted-linker-as-an-integral-part-of-the-catalytic-domain
#18
Henrik Hansson, Saeid Karkehabadi, Nils Mikkelsen, Nicholai R Douglas, Steve Kim, Anna Lam, Thijs Kaper, Brad Kelemen, Katlyn K Meier, Stephen M Jones, Edward I Solomon, Mats Sandgren
For decades, the enzymes of the fungus Hypocrea jecorina have served as a model system for the breakdown of cellulose. Three-dimensional structures for almost all H. jecorina cellulose-degrading enzymes are available, except for HjLPMO9A, belonging to the AA9 family of lytic polysaccharide monooxygenases (LPMOs). These enzymes enhance the hydrolytic activity of cellulases and are essential for cost-efficient conversion of lignocellulosic biomass. Here, using structural and spectroscopic analyses, we found that native HjLPMO9A contains a catalytic domain and a family-1 carbohydrate-binding module (CBM1) connected via a linker sequence...
September 12, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28887418/chitinase-expression-in-listeria-monocytogenes-is-influenced-by-lmo0327-which-encodes-an-internalin-like-protein
#19
Dafni Katerina Paspaliari, Vicky Gaedt Kastbjerg, Hanne Ingmer, Magdalena Popowska, Marianne Halberg Larsen
The chitinolytic system of Listeria monocytogenes thus far comprises two chitinases, ChiA and ChiB, and a lytic polysaccharide monooxygenase, Lmo2467. The role of the system in the bacterium appears to be pleiotropic, as besides mediating the hydrolysis of chitin, the second most ubiquitous carbohydrate in nature, the chitinases have been deemed important for the colonization of unicellular molds, as well as mammalian hosts. To identify additional components of the chitinolytic system, we screened a transposon mutant library for mutants exhibiting impaired chitin hydrolysis...
November 15, 2017: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/28884316/improving-extracellular-production-of-serratia-marcescens-lytic-polysaccharide-monooxygenase-cbp21-and-aeromonas-veronii-b565-chitinase-chi92-in-escherichia-coli-and-their-synergism
#20
Yalin Yang, Juan Li, Xuewei Liu, Xingliang Pan, Junxiu Hou, Chao Ran, Zhigang Zhou
Lytic polysaccharide monooxygenases (LPMOs) can oxidize recalcitrant polysaccharides and boost the conversion of the second most abundant polysaccharide chitin by chitinase. In this study, we aimed to achieve the efficient extracellular production of Serratia marcescens LPMO CBP21 and Aeromonas veronii B565 chitinase Chi92 by Escherichia coli. Twelve signal peptides reported with high secretion efficiency were screened to assess the extracellular production efficiency of CBP21 and Chi92, with glycine used as a medium supplement...
September 7, 2017: AMB Express
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