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https://www.readbyqxmd.com/read/29453372/enzyme-mediated-nanofibrillation-of-cellulose-by-the-synergistic-actions-of-an-endoglucanase-lytic-polysaccharide-monooxygenase-lpmo-and-xylanase
#1
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
https://www.readbyqxmd.com/read/29377002/lytic-xylan-oxidases-from-wood-decay-fungi-unlock-biomass-degradation
#2
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
https://www.readbyqxmd.com/read/29374564/structural-investigation-of-cellobiose-dehydrogenase-iia-insights-from-small-angle-scattering-into-intra-and-intermolecular-electron-transfer-mechanisms
#3
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
https://www.readbyqxmd.com/read/29371886/laccase-derived-lignin-compounds-boost-cellulose-oxidative-enzymes-aa9
#4
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
https://www.readbyqxmd.com/read/29259205/action-of-lytic-polysaccharide-monooxygenase-on-plant-tissue-is-governed-by-cellular-type
#5
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
#6
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
#7
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
#8
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/29228039/biochemical-studies-of-two-lytic-polysaccharide-monooxygenases-from-the-white-rot-fungus-heterobasidion-irregulare-and-their-roles-in-lignocellulose-degradation
#9
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
#10
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/29158777/combined-genome-and-transcriptome-sequencing-to-investigate-the-plant-cell-wall-degrading-enzyme-system-in-the-thermophilic-fungus-malbranchea-cinnamomea
#11
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/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/29026070/single-molecule-study-of-oxidative-enzymatic-deconstruction-of-cellulose
#14
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
#15
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/28884316/improving-extracellular-production-of-serratia-marcescens-lytic-polysaccharide-monooxygenase-cbp21-and-aeromonas-veronii-b565-chitinase-chi92-in-escherichia-coli-and-their-synergism
#16
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
https://www.readbyqxmd.com/read/28827309/withdrawn-identification-of-an-endogenous-redox-partner-for-lytic-polysaccharide-monooxygenase-based-oxidative-cleavage-of-polysaccharides
#17
Nidhi Adlakha, Girish H Rajacharya, Rakesh Bhatnagar
This article has been withdrawn by the authors. Figs 4B and 6C were inappropriately presented.
August 21, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28750348/a-comparative-study-on-the-activity-of-fungal-lytic-polysaccharide-monooxygenases-for-the-depolymerization-of-cellulose-in-soybean-spent-flakes
#18
Brian C Pierce, Jane Wittrup Agger, Zhenghong Zhang, Jesper Wichmann, Anne S Meyer
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes capable of the oxidative breakdown of polysaccharides. They are of industrial interest due to their ability to enhance the enzymatic depolymerization of recalcitrant substrates by glycoside hydrolases. In this paper, twenty-four lytic polysaccharide monooxygenases (LPMOs) expressed in Trichoderma reesei were evaluated for their ability to oxidize the complex polysaccharides in soybean spent flakes, an abundant and industrially relevant substrate...
September 8, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28702082/enzymatic-degradation-of-sulfite-pulped-softwoods-and-the-role-of-lpmos
#19
Piotr Chylenski, Dejan M Petrović, Gerdt Müller, Marie Dahlström, Oskar Bengtsson, Martin Lersch, Matti Siika-Aho, Svein Jarle Horn, Vincent G H Eijsink
BACKGROUND: Recent advances in the development of enzyme cocktails for degradation of lignocellulosic biomass, especially the discovery of lytic polysaccharide monooxygenases (LPMOs), have opened new perspectives for process design and optimization. Softwood biomass is an abundant resource in many parts of the world, including Scandinavia, but efficient pretreatment and subsequent enzymatic hydrolysis of softwoods are challenging. Sulfite pulping-based pretreatments, such as in the BALI™ process, yield substrates that are relatively easy to degrade...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28698982/targeting-the-reactive-intermediate-in-polysaccharide-monooxygenases
#20
Erik D Hedegård, Ulf Ryde
Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism, making them interesting for the production of biofuel from cellulose. However, the details of this activation are unknown; in particular, the nature of the intermediate that attacks the glycoside C-H bond in the polysaccharide is not known, and a number of different species have been suggested. The homolytic bond-dissociation energy (BDE) has often been used as a descriptor for the bond-activation power, especially for inorganic model complexes...
October 2017: Journal of Biological Inorganic Chemistry: JBIC
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