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Polysaccharide monooxygenase

Jian Du, Wenxia Song, Xiu Zhang, Jian Zhao, Guodong Liu, Yinbo Qu
High dosage of enzyme is required to achieve effective lignocellulose hydrolysis, especially at high-solid loadings, which is a significant barrier to large-scale bioconversion of lignocellulose. Here, we screened four chemical additives and three accessory proteins for their effects on the enzymatic hydrolysis of various lignocellulosic materials. The effects were found to be highly dependent on the composition and solid loadings of substrates. For xylan-extracted lignin-rich corncob residue, the enhancing effect of PEG 6000 was most pronounced and negligibly affected by solid content, which reduced more than half of enzyme demand at 20% dry matter (DM)...
April 23, 2018: Bioprocess and Biosystems Engineering
John A Hangasky, Anthony T Iavarone, Michael A Marletta
Enzymatic conversion of polysaccharides into lower-molecular-weight, soluble oligosaccharides is dependent on the action of hydrolytic and oxidative enzymes. Polysaccharide monooxygenases (PMOs) use an oxidative mechanism to break the glycosidic bond of polymeric carbohydrates, thereby disrupting the crystalline packing and creating new chain ends for hydrolases to depolymerize and degrade recalcitrant polysaccharides. PMOs contain a mononuclear Cu(II) center that is directly involved in C-H bond hydroxylation...
April 23, 2018: Proceedings of the National Academy of Sciences of the United States of America
John Hangasky, Michael A Marletta
Polysaccharide monooxygenases are mononuclear copper enzymes that catalyze the hydroxylation of polysaccharides leading to the scission of the glycosidic bond. The mechanism in which PMOs utilize molecular oxygen to oxidize the polysaccharide substrate still remains largely unknown. Here, steady-state kinetics assays were used to probe the mechanism of oxygen-dependent cellohexaose oxidation catalyzed by MtPMO9E. Kinetic analysis indicated that both kcat /KM (O2 ) and kcat/KM(Glc6) were dependent on the concentration of the second substrate...
April 23, 2018: Biochemistry
Bing Liu, Abhishek A Kognole, Miao Wu, Bjørge Westereng, Michael F Crowley, Seonah Kim, Maria Dimarogona, Christina M Payne, Mats Sandgren
Lytic polysaccharide monooxygenases (LPMOs) are a group of recently discovered enzymes that play important roles in the decomposition of recalcitrant polysaccharides. Here, we report the biochemical, structural and computational characterization of an LPMO from the white-rot fungus Heterobasidion irregulare (HiLPMO9B). This enzyme oxidizes cellulose at the C1 carbon of glycosidic linkages. The crystal structure of HiLPMO9B was determined at 2.1 Å resolution using X-ray crystallography. Unlike the majority of the currently available C1-specific LPMO structures, the HiLPMO9B structure contains an extended L2 loop, connecting β-strands β2 and β3 of the β-sandwich structure...
April 16, 2018: FEBS Journal
Paula Fagundes de Gouvêa, Aline Vianna Bernardi, Luis Eduardo Gerolamo, Emerson de Souza Santos, Diego Mauricio Riaño-Pachón, Sergio Akira Uyemura, Taisa Magnani Dinamarco
BACKGROUND: Sugarcane bagasse has been proposed as a lignocellulosic residue for second-generation ethanol (2G) produced by breaking down biomass into fermentable sugars. The enzymatic cocktails for biomass degradation are mostly produced by fungi, but low cost and high efficiency can consolidate 2G technologies. A. fumigatus plays an important role in plant biomass degradation capabilities and recycling. To gain more insight into the divergence in gene expression during steam-exploded bagasse (SEB) breakdown, this study profiled the transcriptome of A...
April 3, 2018: BMC Genomics
Anikó Várnai, Kiwamu Umezawa, Makoto Yoshida, Vincent G H Eijsink
Fungi secrete a set of glycoside hydrolases and oxidoreductases, including lytic polysaccharide monooxygenases (LPMOs), for the degradation of plant polysaccharides. LPMOs catalyze the oxidative cleavage of glycosidic bonds after activation by an external electron donor. So far, only flavin-dependent oxidoreductases (from the auxiliary activity family AA3) have been shown to activate LPMOs. Here we present LPMO activation by a pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase (PDH) from Coprinopsis cinerea , Cc PDH, the founding member of the recently discovered auxiliary activity family AA12...
March 30, 2018: Applied and Environmental Microbiology
Cynthia Sanhueza, Gonzalo Carvajal, Javiera Soto-Aguilar, Maria Elena Lienqueo, Oriana Salazar
Hydrolysis of lignocellulosic biomass depends on the concerted actions of cellulases and accessory proteins. In this work we examined the combined action of two auxiliary proteins from the brown rot fungus Gloeophyllum trabeum: a family AA9 lytic polysaccharide monooxygenase (GtLPMO) and a GH10 xylanase (GtXyn10A). The enzymes were produced in the heterologous host Pichia pastoris. In the presence of an electron source, GtLPMO increased the activity of a commercial cellulase on filter paper, and the xylanase activity of GtXyn10A on beechwood xylan...
June 2018: Enzyme and Microbial Technology
Erik Breslmayr, Marija Hanžek, Aoife Hanrahan, Christian Leitner, Roman Kittl, Božidar Šantek, Chris Oostenbrink, Roland Ludwig
Background: Lytic polysaccharide monooxygenases (LPMO) release a spectrum of cleavage products from their polymeric substrates cellulose, hemicellulose, or chitin. The correct identification and quantitation of these released products is the basis of MS/HPLC-based detection methods for LPMO activity. The duration, effort, and intricate analysis allow only specialized laboratories to measure LPMO activity in day-to-day work. A spectrophotometric assay will simplify the screening for LPMO in culture supernatants, help monitor recombinant LPMO expression and purification, and support enzyme characterization...
2018: Biotechnology for Biofuels
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 monocopper 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 multidisciplinary approach, combining biochemical, spectroscopic, and molecular modeling methods to study chitin binding by the well-studied LPMO from Serratia marcescens SmAA10A (or CBP21)...
March 27, 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...
April 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...
March 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)...
April 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 toward 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...
February 2, 2018: 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
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