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Polysaccharide monooxygenase

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https://www.readbyqxmd.com/read/28341558/biomethane-the-energy-storage-platform-chemical-and-greenhouse-gas-mitigation-target
#1
Zoltán Bagi, Norbert Ács, Tamás Böjti, Balázs Kakuk, Gábor Rákhely, Orsolya Strang, Márk Szuhaj, Roland Wirth, Kornél L Kovács
Results in three areas of anaerobic microbiology in which methane formation and utilization plays central part are reviewed. a.) Bio-methane formation by reduction of carbon dioxide in the power-to-gas process and the various possibilities of improvement of the process is a very intensively studied topic recently. From the numerous potential methods of exploiting methane of biological origin two aspects are discussed in detail. b.) Methane can serve as a platform chemical in various chemical and biochemical synthetic processes...
March 21, 2017: Anaerobe
https://www.readbyqxmd.com/read/28338903/disulfide-bridges-as-essential-elements-for-the-thermostability-of-lytic-polysaccharide-monooxygenase-lpmo10c-from-streptomyces-coelicolor
#2
Magali Tanghe, Barbara Danneels, Matthias Last, Koen Beerens, Ingeborg Stals, Tom Desmet
Lytic polysaccharide monooxygenases (LPMOs) are crucial components of cellulase mixtures but their stability has not yet been studied in detail, let alone been engineered for industrial applications. In this work, we have evaluated the importance of disulfide bridges for the thermodynamic stability of Streptomyces coelicolor LPMO10C. Interestingly, this enzyme was found to retain 34% of its activity after 2-h incubation at 80°C while its apparent melting temperature (Tm) is only 51°C. When its three disulfide bridges were broken, however, irreversible unfolding occurred and no residual activity could be detected after a similar heat treatment...
March 9, 2017: Protein Engineering, Design & Selection: PEDS
https://www.readbyqxmd.com/read/28335986/on-the-formation-and-role-of-reactive-oxygen-species-in-light-driven-lpmo-oxidation-of-phosphoric-acid-swollen-cellulose
#3
K B Möllers, H Mikkelsen, T I Simonsen, D Cannella, K S Johansen, M J Bjerrum, C Felby
Light-driven activation of lytic polysaccharide monooxygenases (LPMOs) has been attributed to the transfer of high redox potential electrons from excited photopigments to the enzyme. However, due to the formation of reactive oxygen species (ROS) in such a system, not only electrons from the pigments but also ROS could be part of the enzyme mechanism. This work investigates the role of ROS in the oxidation of phosphoric acid swollen cellulose (PASC) by a light-driven LPMO system. Our results clearly show that the addition of superoxide dismutase or catalase to remove ROS did not attenuate the capacity of the light-driven LPMO system to oxidize PASC, as measured by formation of oxidized oligosaccharides...
March 18, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28302276/rp-uhplc-uv-esi-ms-ms-analysis-of-lpmo-generated-c4-oxidized-gluco-oligosaccharides-after-non-reductive-labeling-with-2-aminobenzamide
#4
Matthias Frommhagen, Gijs van Erven, Mark Sanders, Willem J H van Berkel, Mirjam A Kabel, Harry Gruppen
Lytic polysaccharide monooxygenases (LPMOs) are able to cleave recalcitrant polysaccharides, such as cellulose, by oxidizing the C1 and/or C4 atoms. The analysis of the resulting products requires a variety of analytical techniques. Up to now, these techniques mainly focused on the identification of non-oxidized and C1-oxidized oligosaccharides. The analysis of C4-oxidized gluco-oligosaccharides is mostly performed by using high pressure anion exchange chromatography (HPAEC). However, the alkaline conditions used during HPAEC analysis lead to tautomerization of C4-oxidized gluco-oligosaccharides, which limits the use of this technique...
March 6, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28293293/the-podospora-anserina-lytic-polysaccharide-monooxygenase-palpmo9h-catalyzes-oxidative-cleavage-of-diverse-plant-cell-wall-matrix-glycans
#5
Mathieu Fanuel, Sona Garajova, David Ropartz, Nicholas McGregor, Harry Brumer, Hélène Rogniaux, Jean-Guy Berrin
BACKGROUND: The enzymatic conversion of plant biomass has been recently revolutionized by the discovery of lytic polysaccharide monooxygenases (LPMO) that catalyze oxidative cleavage of polysaccharides. These powerful enzymes are secreted by a large number of fungal saprotrophs and are important components of commercial enzyme cocktails used for industrial biomass conversion. Among the 33 AA9 LPMOs encoded by the genome of Podospora anserina, the PaLPMO9H enzyme catalyzes mixed C1/C4 oxidative cleavage of cellulose and cello-oligosaccharides...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28291519/structural-studies-of-neurospora-crassa-lpmo9d-and-redox-partner-cdhiia-using-neutron-crystallography-and-small-angle-scattering
#6
Annette M Bodenheimer, William B O'Dell, Christopher B Stanley, Flora Meilleur
Sensitivity to hydrogen/deuterium and lack of observable radiation damage makes cold neutrons an ideal probe the structural studies of proteins with highly photosensitive groups such as the copper center of lytic polysaccharide monooxygenases (LPMOs) and flavin adenine dinucleotide (FAD) and heme redox cofactors of cellobiose dehydrogenases (CDHs). Here, neutron crystallography and small-angle neutron scattering are used to investigate Neurospora crassa LPMO9D (NcLPMO9D) and CDHIIA (NcCDHIIA), respectively...
March 4, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28291518/a-novel-expression-system-for-lytic-polysaccharide-monooxygenases
#7
Gaston Courtade, Simone Balzer Le, Gerd Inger Sætrom, Trygve Brautaset, Finn L Aachmann
Lytic polysaccharide monooxygenases (LPMOs) are key enzymatic players of lignocellulosic biomass degradation processes. As such, they have been introduced in cellulolytic cocktails for more efficient and less expensive lignocellulose saccharification. The recombinant production of LPMOs in bacteria for scientific investigations using vectors typically based on the T7 and lacUV5 promoters has been hampered by low yields. Reasons for this have been catabolite repression when producing the proteins in defined media with glucose as the sole carbon source, as well as the lack of an inducible expression system that allows controlled production of LPMOs that are correctly processed during translocation to the periplasmic space...
February 14, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28257189/the-role-of-the-secondary-coordination-sphere-in-a-fungal-polysaccharide-monooxygenase
#8
Elise A Span, Daniel L M Suess, Marc C Deller, R David Britt, Michael A Marletta
Polysaccharide monooxygenases (PMOs) are secreted metalloenzymes that catalyze the oxidative degradation of polysaccharides in a copper-, oxygen-, and reductant-dependent manner. Cellulose-active fungal PMOs degrade cellulosic substrates to be utilized as a carbon source for fungal growth. To gain insight into the PMO mechanism, the role of conserved residues in the copper coordination sphere was investigated. Here, we report active-site hydrogen-bonding motifs in the secondary copper coordination sphere of MtPMO3*, a C1-oxidizing PMO from the ascomycete fungus Myceliophthora thermophila...
March 3, 2017: ACS Chemical Biology
https://www.readbyqxmd.com/read/28250814/type-dependent-action-modes-of-ttaa9e-and-taaa9a-acting-on-cellulose-and-differently-pretreated-lignocellulosic-substrates
#9
In Jung Kim, Nari Seo, Hyun Joo An, Jae-Han Kim, Paul V Harris, Kyoung Heon Kim
BACKGROUND: Lytic polysaccharide monooxygenase (LPMO) is a group of recently identified proteins that catalyze oxidative cleavage of the glycosidic linkages of cellulose and other polysaccharides. By utilizing the oxidative mode of action, LPMOs are able to enhance the efficiency of cellulase in the hydrolysis of cellulose. Particularly, auxiliary activity family 9 (AA9) is a group of fungal LPMOs that show a type-dependent regioselectivity on cellulose in which Types 1, 2, and 3 hydroxylate at C1, C4, and C1 and C4 positions, respectively...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28219736/development-of-minimal-enzyme-cocktails-for-hydrolysis-of-sulfite-pulped-lignocellulosic-biomass
#10
Piotr Chylenski, Zarah Forsberg, Jerry Ståhlberg, Anikó Várnai, Martin Lersch, Oskar Bengtsson, Solve Sæbø, Svein Jarle Horn, Vincent G H Eijsink
Despite recent progress, saccharification of lignocellulosic biomass is still a major cost driver in biorefining. In this study, we present the development of minimal enzyme cocktails for hydrolysis of Norway spruce and sugarcane bagasse, which were pretreated using the so-called BALI™ process, which is based on sulfite pulping technology. Minimal enzyme cocktails were composed using several glycoside hydrolases purified from the industrially relevant filamentous fungus Trichoderma reesei and a purified commercial β-glucosidase from Aspergillus niger...
March 20, 2017: Journal of Biotechnology
https://www.readbyqxmd.com/read/28188936/cultivation-of-podospora-anserina-on-soybean-hulls-results-in-an-efficient-enzyme-cocktail-for-plant-biomass-hydrolysis
#11
Miia R Mäkelä, Ourdia Bouzid, Diogo Robl, Harm Post, Mao Peng, Albert Heck, Maarten Altelaar, Ronald P de Vries
The coprophilic ascomycete fungus Podospora anserina was cultivated on three different plant biomasses, i.e. cotton seed hulls (CSH), soybean hulls (SBH) and acid-pretreated wheat straw (WS) for four days, and the potential of the produced enzyme mixtures was compared in the enzymatic saccharification of the corresponding lignocellulose feedstocks. The enzyme cocktail P. anserina produced after three days of growth on SBH showed superior capacity to release reducing sugars from all tested plant biomass feedstocks compared to the enzyme mixtures from CSH and WS cultures...
February 7, 2017: New Biotechnology
https://www.readbyqxmd.com/read/28177316/crystallization-of-a-fungal-lytic-polysaccharide-monooxygenase-expressed-from-glycoengineered-pichia-pastoris-for-x-ray-and-neutron-diffraction
#12
William B O'Dell, Paul D Swartz, Kevin L Weiss, Flora Meilleur
Lytic polysaccharide monooxygenases (LPMOs) are carbohydrate-disrupting enzymes secreted by bacteria and fungi that break glycosidic bonds via an oxidative mechanism. Fungal LPMOs typically act on cellulose and can enhance the efficiency of cellulose-hydrolyzing enzymes that release soluble sugars for bioethanol production or other industrial uses. The enzyme PMO-2 from Neurospora crassa (NcPMO-2) was heterologously expressed in Pichia pastoris to facilitate crystallographic studies of the fungal LPMO mechanism...
February 1, 2017: Acta Crystallographica. Section F, Structural Biology Communications
https://www.readbyqxmd.com/read/28125213/microplate-based-detection-of-lytic-polysaccharide-monooxygenase-activity-by-fluorescence-labeling-of-insoluble-oxidized-products
#13
Thu V Vuong, Bing Liu, Mats Sandgren, Emma R Master
Most existing methods for screening the activity of lytic polysaccharide mono-oxygenases (LPMOs) on polysaccharides are based on the detection of soluble oxidized sugars. This approach might underestimate the total performance of LPMOs since oxidation events that do not lead to oligosaccharide release are not detected. Using PcLPMO9D as a model enzyme, a microplate-based method has been developed to detect C1-oxidizing LPMO activity by covalently linking a water-soluble fluorophore to oxidized positions within the cellulose fiber...
January 26, 2017: Biomacromolecules
https://www.readbyqxmd.com/read/28110665/oxidative-cleavage-and-hydrolytic-boosting-of-cellulose-in-soybean-spent-flakes-by-trichoderma-reesei-cel61a-lytic-polysaccharide-monooxygenase
#14
Brian C Pierce, Jane Wittrup Agger, Jesper Wichmann, Anne S Meyer
The auxiliary activity family 9 (AA9) copper-dependent lytic polysaccharide monooxygenase (LPMO) from Trichoderma reesei (EG4; TrCel61A) was investigated for its ability to oxidize the complex polysaccharides from soybean. The substrate specificity of the enzyme was assessed against a variety of substrates, including both soy spent flake, a by-product of the soy food industry, and soy spent flake pretreated with sodium hydroxide. Products from enzymatic treatments were analyzed using mass spectrometry and high performance anion exchange chromatography...
March 2017: Enzyme and Microbial Technology
https://www.readbyqxmd.com/read/28107425/using-an-inducible-promoter-of-a-gene-encoding-penicillium-verruculosum-glucoamylase-for-production-of-enzyme-preparations-with-enhanced-cellulase-performance
#15
Alexander G Bulakhov, Pavel V Volkov, Aleksandra M Rozhkova, Alexander V Gusakov, Vitaly A Nemashkalov, Aidar D Satrutdinov, Arkady P Sinitsyn
BACKGROUND: Penicillium verruculosum is an efficient producer of highly active cellulase multienzyme system. One of the approaches for enhancing cellulase performance in hydrolysis of cellulosic substrates is to enrich the reaction system with β -glucosidase and/or accessory enzymes, such as lytic polysaccharide monooxygenases (LPMO) displaying a synergism with cellulases. RESULTS: Genes bglI, encoding β-glucosidase from Aspergillus niger (AnBGL), and eglIV, encoding LPMO (formerly endoglucanase IV) from Trichoderma reesei (TrLPMO), were cloned and expressed by P...
2017: PloS One
https://www.readbyqxmd.com/read/28071716/lytic-polysaccharide-monooxygenases-disrupt-the-cellulose-fibers-structure
#16
Ana Villares, Céline Moreau, Chloé Bennati-Granier, Sona Garajova, Loïc Foucat, Xavier Falourd, Bodo Saake, Jean-Guy Berrin, Bernard Cathala
Lytic polysaccharide monooxygenases (LPMOs) are a class of powerful oxidative enzymes that breakdown recalcitrant polysaccharides such as cellulose. Here we investigate the action of LPMOs on cellulose fibers. After enzymatic treatment and dispersion, LPMO-treated fibers show intense fibrillation. Cellulose structure modifications visualized at different scales indicate that LPMO creates nicking points that trigger the disintegration of the cellulose fibrillar structure with rupture of chains and release of elementary nanofibrils...
January 10, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28060494/copper-complexes-as-bioinspired-models-for-lytic-polysaccharide-monooxygenases
#17
Alda Lisa Concia, Maria Rosa Beccia, Maylis Orio, Francine Terra Ferre, Marciela Scarpellini, Frédéric Biaso, Bruno Guigliarelli, Marius Réglier, A Jalila Simaan
We report here two copper complexes as first functional models for lytic polysaccharide monooxygenases, mononuclear copper-containing enzymes involved in recalcitrant polysaccharide breakdown. These complexes feature structural and spectroscopic properties similar to those of the enzyme. In addition, they catalyze oxidative cleavage of the model substrate p-nitrophenyl-β-d-glucopyranoside. More importantly, a particularly stable copper(II) hydroperoxide intermediate is detected in the reaction conditions.
January 6, 2017: Inorganic Chemistry
https://www.readbyqxmd.com/read/28045386/learning-from-oligosaccharide-soaks-of-crystals-of-an-aa13-lytic-polysaccharide-monooxygenase-crystal-packing-ligand-binding-and-active-site-disorder
#18
Kristian E H Frandsen, Jens Christian Navarro Poulsen, Morten Tovborg, Katja S Johansen, Leila Lo Leggio
Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes discovered within the last ten years. They oxidatively cleave polysaccharides (chitin, lignocellulose, hemicellulose and starch-derived), presumably making recalcitrant substrates accessible to glycoside hydrolases. Recently, the first crystal structure of an LPMO-substrate complex was reported, giving insights into the interaction of LPMOs with β-linked substrates (Frandsen et al., 2016). The LPMOs acting on α-linked glycosidic bonds (family AA13) display binding surfaces that are quite different from those of LPMOs that act on β-linked glycosidic bonds (families AA9-AA11), as revealed from the first determined structure (Lo Leggio et al...
January 1, 2017: Acta Crystallographica. Section D, Structural Biology
https://www.readbyqxmd.com/read/28004877/oxygen-activation-at-the-active-site-of-a-fungal-lytic-polysaccharide-monooxygenase
#19
William B O'Dell, Pratul K Agarwal, Flora Meilleur
Lytic polysaccharide monooxygenases have attracted vast attention owing to their abilities to disrupt glycosidic bonds via oxidation instead of hydrolysis and to enhance enzymatic digestion of recalcitrant substrates including chitin and cellulose. We have determined high-resolution X-ray crystal structures of an enzyme from Neurospora crassa in the resting state and of a copper(II) dioxo intermediate complex formed in the absence of substrate. X-ray crystal structures also revealed "pre-bound" molecular oxygen adjacent to the active site...
January 16, 2017: Angewandte Chemie
https://www.readbyqxmd.com/read/27868112/uplc-ms-ms-investigation-of-%C3%AE-glucan-oligosaccharide-oxidation
#20
Samy Boulos, Laura Nyström
Polysaccharide degradation mediated by hydroxyl radicals (HO˙) or lytic monooxygenases (LPMOs) is relevant in various biological and industrial processes. Thereby, the Fenton-induced (H2O2/Fe(2+)) oxidation of mixed-linkage (1→3,1→4)-β-d-glucan (BG), a cereal dietary fibre with several well-established health promoting properties, shows potential for modulating BG functionality. The precise identification of oxidation products, however, is impeded by their diversity due to the indiscriminate nature of HO˙, the large molecular weight, and the corresponding low frequency of discrete alterations along the polymer chain...
November 21, 2016: Analyst
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