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https://www.readbyqxmd.com/read/28919928/the-yeast-geotrichum-candidum-encodes-functional-lytic-polysaccharide-monooxygenases
#1
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
#2
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https://www.readbyqxmd.com/read/28827309/withdrawn-identification-of-an-endogenous-redox-partner-for-lytic-polysaccharide-monooxygenase-based-oxidative-cleavage-of-polysaccharides
#3
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This article has been withdrawn by the authors.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
#4
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/28734034/protein-features-as-determinants-of-wild-type-glycoside-hydrolase-thermostability
#5
Henrik Marcus Geertz-Hansen, Lars Kiemer, Morten Nielsen, Kiril Stanchev, Nikolaj Blom, Søren Brunak, Thomas Nordahl Petersen
Thermostable enzymes for conversion of lignocellulosic biomass into biofuels have significant advantages over enzymes with more moderate themostability due to the challenging application conditions. Experimental discovery of thermostable enzymes is highly cost intensive, and the development of in-silico methods guiding the discovery process would be of high value. To develop such an in-silico method and provide the data foundation of it, we determined the melting temperatures of 602 fungal glycoside hydrolases from the families GH5, 6, 7, 10, 11, 43 and AA9 (formerly GH61)...
July 22, 2017: Proteins
https://www.readbyqxmd.com/read/28559926/genome-wide-characterization-of-cellulases-from-the-hemi-biotrophic-plant-pathogen-bipolaris-sorokiniana-reveals-the-presence-of-a-highly-stable-gh7-endoglucanase
#6
Shritama Aich, Ravi K Singh, Pritha Kundu, Shree P Pandey, Supratim Datta
BACKGROUND: Bipolaris sorokiniana is a filamentous fungus that causes spot blotch disease in cereals like wheat and has severe economic consequences. However, information on the identities and role of the cell wall-degrading enzymes (CWDE) in B. sorokiniana is very limited. Several fungi produce CWDE like glycosyl hydrolases (GHs) that help in host cell invasion. To understand the role of these CWDE in B. sorokiniana, the first step is to identify and annotate all possible genes of the GH families like GH3, GH6, GH7, GH45 and AA9 and then characterize them biochemically...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28491137/boosting-lpmo-driven-lignocellulose-degradation-by-polyphenol-oxidase-activated-lignin-building-blocks
#7
Matthias Frommhagen, Sumanth Kumar Mutte, Adrie H Westphal, Martijn J Koetsier, Sandra W A Hinz, Jaap Visser, Jean-Paul Vincken, Dolf Weijers, Willem J H van Berkel, Harry Gruppen, Mirjam A Kabel
BACKGROUND: Many fungi boost the deconstruction of lignocellulosic plant biomass via oxidation using lytic polysaccharide monooxygenases (LPMOs). The application of LPMOs is expected to contribute to ecologically friendly conversion of biomass into fuels and chemicals. Moreover, applications of LPMO-modified cellulose-based products may be envisaged within the food or material industry. RESULTS: Here, we show an up to 75-fold improvement in LPMO-driven cellulose degradation using polyphenol oxidase-activated lignin building blocks...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28450248/fungal-lytic-polysaccharide-monooxygenases-from-family-aa9-recent-developments-and-application-in-lignocelullose-breakdown
#8
REVIEW
Antonielle Vieira Monclaro, Edivaldo Ximenes Ferreira Filho
Fungal lytic polysaccharide monooxygenases (LPMOs) from family AA9 are oxidative enzymes that, in the past few years, have changed the paradigm of cellulose conversion. They are key factor in the lignocellulose breakdown and are widely distributed among fungi. This review focuses on LPMOs from family AA9 and gives an overview of recent discoveries relative to their structure, mode of action, and synergism with other enzymes. Finally, several aspects regarding their potential applications toward deconstruction of biomass and biorefinery processes are discussed...
September 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/28434716/a-bioinformatics-analysis-of-3400-lytic-polysaccharide-oxidases-from-family-aa9
#9
Nicolas Lenfant, Matthieu Hainaut, Nicolas Terrapon, Elodie Drula, Vincent Lombard, Bernard Henrissat
Lytic polysaccharide monooxygenases of family AA9 catalyze the oxidative cleavage of glycosidic bonds in cellulose and related polysaccharides. The N-terminal half of AA9 LPMOs displays a huge sequence variability that is in contradiction with the substrate simplicity so far observed for these enzymes. To understand the cause of the high multigenicity that prevails in the family, we have performed a clustering analysis of the N-terminal region of 3400 sequences of family AA9 LPMOs, and have evaluated the coincidence of the clusters with distal visible features that may accompany functional differences...
April 13, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28364950/unliganded-and-substrate-bound-structures-of-the-cellooligosaccharide-active-lytic-polysaccharide-monooxygenase-lsaa9a-at-low-ph
#10
Kristian E H Frandsen, Jens-Christian N Poulsen, Tobias Tandrup, Leila Lo Leggio
Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3...
March 24, 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
#11
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/28250814/type-dependent-action-modes-of-ttaa9e-and-taaa9a-acting-on-cellulose-and-differently-pretreated-lignocellulosic-substrates
#12
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/28188936/cultivation-of-podospora-anserina-on-soybean-hulls-results-in-an-efficient-enzyme-cocktail-for-plant-biomass-hydrolysis
#13
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...
July 25, 2017: New Biotechnology
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/28045386/learning-from-oligosaccharide-soaks-of-crystals-of-an-aa13-lytic-polysaccharide-monooxygenase-crystal-packing-ligand-binding-and-active-site-disorder
#15
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/27919659/synthesis-and-sar-study-of-novel-sarsasapogenin-derivatives-as-potent-neuroprotective-agents-and-no-production-inhibitors
#16
Hui Pan, Pham Van Khang, Dong Dong, Rui Wang, Lei Ma
Sarsasapogenin, isolated from rhizomes of Anemarrhena asphodeloides, was found to be able to enhance memory. On the basis of the structure of Sarsasapogenin, a series of derivatives were synthesized and evaluated for their neuroprotective activity in PC12 cells and NO production inhibitory activity in RAW264.7 cell lines. The preliminary structure-activity relationship of them indicated that introduction of carbamate groups at the 3-hydroxyl position of sarsasapogenin might improve neuroprotective activity...
February 1, 2017: Bioorganic & Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/27833654/bioinformatic-characterization-of-type-specific-sequence-and-structural-features-in-auxiliary-activity-family-9-proteins
#17
Vuyani Moses, Rowan Hatherley, Özlem Tastan Bishop
BACKGROUND: Due to the impending depletion of fossil fuels, it has become important to identify alternative energy sources. The biofuel industry has proven to be a promising alternative. However, owing to the complex nature of plant biomass, hence the degradation, biofuel production remains a challenge. The copper-dependent Auxiliary Activity family 9 (AA9) proteins have been found to act synergistically with other cellulose-degrading enzymes resulting in an increased rate of cellulose breakdown...
2016: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/27744242/mycothermus-thermophilus-syn-scytalidium-thermophilum-repertoire-of-a-diverse-array-of-efficient-cellulases-and-hemicellulases-in-the-secretome-revealed
#18
Neha Basotra, Baljit Kaur, Marcos Di Falco, Adrian Tsang, Bhupinder Singh Chadha
Mycothermus thermophilus (Syn. Scytalidium thermophilum/Humicola insolens), a thermophilic fungus, is being reported to produce appreciable titers of cellulases and hemicellulases during shake flask culturing on cellulose/wheat-bran/rice straw based production medium. The sequential and differential expression profile of endoglucanases, β-glucosidases, cellobiohydrolases and xylanases using zymography was studied. Mass spectrometry analysis of secretome (Q-TOF LC/MS) revealed a total of 240 proteins with 92 CAZymes of which 62 glycosyl hydrolases belonging to 30 different families were present...
December 2016: Bioresource Technology
https://www.readbyqxmd.com/read/27602055/time-scale-dynamics-of-proteome-and-transcriptome-of-the-white-rot-fungus-phlebia-radiata-growth-on-spruce-wood-and-decay-effect-on-lignocellulose
#19
Jaana Kuuskeri, Mari Häkkinen, Pia Laine, Olli-Pekka Smolander, Fitsum Tamene, Sini Miettinen, Paula Nousiainen, Marianna Kemell, Petri Auvinen, Taina Lundell
BACKGROUND: The white-rot Agaricomycetes species Phlebia radiata is an efficient wood-decaying fungus degrading all wood components, including cellulose, hemicellulose, and lignin. We cultivated P. radiata in solid state cultures on spruce wood, and extended the experiment to 6 weeks to gain more knowledge on the time-scale dynamics of protein expression upon growth and wood decay. Total proteome and transcriptome of P. radiata were analyzed by peptide LC-MS/MS and RNA sequencing at specific time points to study the enzymatic machinery on the fungus' natural growth substrate...
2016: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/27590806/characterization-of-an-lpmo-from-the-brown-rot-fungus-gloeophyllum-trabeum-with-broad-xyloglucan-specificity-and-its-action-on-cellulose-xyloglucan-complexes
#20
Yuka Kojima, Anikó Várnai, Takuya Ishida, Naoki Sunagawa, Dejan M Petrovic, Kiyohiko Igarashi, Jody Jellison, Barry Goodell, Gry Alfredsen, Bjørge Westereng, Vincent G H Eijsink, Makoto Yoshida
Fungi secrete a set of glycoside hydrolases and lytic polysaccharide monooxygenases (LPMOs) to degrade plant polysaccharides. Brown-rot fungi, such as Gloeophyllum trabeum, tend to have few LPMOs and information on these enzymes is scarce. The genome of G. trabeum encodes four AA9 LPMOs, whose coding sequences were amplified from cDNA. Due to alternative splicing, two variants of GtLPMO9A seem to be produced, a single domain variant, GtLPMO9A-1, and a longer variant, GtLPMO9A-2, which contains a C-terminal domain comprising approximately 55 residues without a predicted function...
September 2, 2016: Applied and Environmental Microbiology
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