keyword
MENU ▼
Read by QxMD icon Read
search

Aa9

keyword
https://www.readbyqxmd.com/read/29614953/transcriptome-and-secretome-analysis-of-aspergillus-fumigatus-in-the-presence-of-sugarcane-bagasse
#1
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
https://www.readbyqxmd.com/read/29602390/the-effect-of-a-lytic-polysaccharide-monooxygenase-and-a-xylanase-from-gloeophyllum-trabeum-on-the-enzymatic-hydrolysis-of-lignocellulosic-residues-using-a-commercial-cellulase
#2
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
https://www.readbyqxmd.com/read/29371886/laccase-derived-lignin-compounds-boost-cellulose-oxidative-enzymes-aa9
#3
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
#4
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/29232119/catalytic-mechanism-of-fungal-lytic-polysaccharide-monooxygenases-investigated-by-first-principles-calculations
#5
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...
January 2, 2018: 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
#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/29158777/combined-genome-and-transcriptome-sequencing-to-investigate-the-plant-cell-wall-degrading-enzyme-system-in-the-thermophilic-fungus-malbranchea-cinnamomea
#7
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/29057953/structural-and-electronic-determinants-of-lytic-polysaccharide-monooxygenase-reactivity-on-polysaccharide-substrates
#8
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/29025413/carbohydrate-active-enzymes-in-trichoderma-harzianum-a-bioinformatic-analysis-bioprospecting-for-key-enzymes-for-the-biofuels-industry
#9
Jaire Alves Ferreira Filho, Maria Augusta Crivelente Horta, Lilian Luzia Beloti, Clelton Aparecido Dos Santos, Anete Pereira de Souza
BACKGROUND: Trichoderma harzianum is used in biotechnology applications due to its ability to produce powerful enzymes for the conversion of lignocellulosic substrates into soluble sugars. Active enzymes involved in carbohydrate metabolism are defined as carbohydrate-active enzymes (CAZymes), and the most abundant family in the CAZy database is the glycoside hydrolases. The enzymes of this family play a fundamental role in the decomposition of plant biomass. RESULTS: In this study, the CAZymes of T...
October 12, 2017: BMC Genomics
https://www.readbyqxmd.com/read/28919928/the-yeast-geotrichum-candidum-encodes-functional-lytic-polysaccharide-monooxygenases
#10
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
#11
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 Hj LPMO9A, 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 Hj LPMO9A contains a catalytic domain and a family-1 carbohydrate-binding module (CBM1) connected via a linker sequence...
November 17, 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
#12
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
#13
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
#14
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)...
November 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
#15
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
#16
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
#17
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
#18
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
#19
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
#20
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
keyword
keyword
74394
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"