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https://www.readbyqxmd.com/read/29222333/structural-determinants-of-bacterial-lytic-polysaccharide-monooxygenase-functionality
#1
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
#2
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
#3
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
#4
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
#5
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
#6
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
#7
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
#8
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
#9
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
#10
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
#11
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
https://www.readbyqxmd.com/read/28535872/fungal-secretomics-to-probe-the-biological-functions-of-lytic-polysaccharide-monooxygenases
#12
Jean-Guy Berrin, Marie-Noëlle Rosso, Maher Abou Hachem
Enzymatic degradation of plant biomass is of growing interest for the development of a sustainable bio-based industry. Filamentous fungi, which degrade complex and recalcitrant plant polymers, are proficient secretors of enzymes acting on the lignocellulose composite of plant cell walls in addition to starch, the main carbon storage reservoir. In this review, we focus on the identification of lytic polysaccharide monooxygenases (LPMOs) and their redox partners in fungal secretomes to highlight the biological functions of these remarkable enzyme systems and we discuss future trends related to LPMO-potentiated bioconversion...
May 17, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28515785/recombinant-expression-of-thermostable-processive-mteg5-endoglucanase-and-its-synergism-with-mtlpmo-from-myceliophthora-thermophila-during-the-hydrolysis-of-lignocellulosic-substrates
#13
Anthi Karnaouri, Madhu Nair Muraleedharan, Maria Dimarogona, Evangelos Topakas, Ulrika Rova, Mats Sandgren, Paul Christakopoulos
BACKGROUND: Filamentous fungi are among the most powerful cellulolytic organisms in terrestrial ecosystems. To perform the degradation of lignocellulosic substrates, these microorganisms employ both hydrolytic and oxidative mechanisms that involve the secretion and synergism of a wide variety of enzymes. Interactions between these enzymes occur on the level of saccharification, i.e., the release of neutral and oxidized products, but sometimes also reflected in the substrate liquefaction...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28491137/boosting-lpmo-driven-lignocellulose-degradation-by-polyphenol-oxidase-activated-lignin-building-blocks
#14
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/28434716/a-bioinformatics-analysis-of-3400-lytic-polysaccharide-oxidases-from-family-aa9
#15
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/28417362/analyzing-activities-of-lytic-polysaccharide-monooxygenases-by-liquid-chromatography-and-mass-spectrometry
#16
Bjørge Westereng, Magnus Ø Arntzen, Jane Wittrup Agger, Gustav Vaaje-Kolstad, Vincent G H Eijsink
Lytic polysaccharide monooxygenases perform oxidative cleavage of glycosidic bonds in various polysaccharides. The majority of LMPOs studied so far possess activity on either cellulose or chitin and analysis of these activities is therefore the main focus of this review. Notably, however, the number of LPMOs that are active on other polysaccharides is increasing. The products generated by LPMOs from cellulose are either oxidized in the downstream end (at C1) or upstream end (at C4), or at both ends. These modifications only result in small structural changes, which makes both chromatographic separation and product identification by mass spectrometry challenging...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28411891/recombinant-expression-of-thermobifida-fusca-e7-lpmo-in-pichia-pastoris-and-escherichia-coli-and-their-functional-characterization
#17
Kelly B Rodrigues, Jéssica K A Macêdo, Tallyta Teixeira, Jéssica S Barros, Ana C B Araújo, Fernanda P Santos, Betânia F Quirino, Bruno S A F Brasil, Thaís F C Salum, Patrícia V Abdelnur, Léia C L Fávaro
The discovery of lytic polysaccharides monooxygenases copper dependent (LPMOs) revolutionized the classical concept that the cleavage of cellulose is a hydrolytic process in recent years. These enzymes carry out oxidative cleavage of cellulose (and other polysaccharides), acting synergistically with cellulases and other hydrolases. In fact, LPMOs have the potential for increasing the efficiency of the lignocellulosic biomass conversion in biofuels and high value chemicals. Among a small number of microbial LPMOs that have been characterized, some LPMOs were expressed and characterized biochemically from the bacteria Thermobifida fusca, using the host Escherichia coli...
April 9, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28394946/the-integrative-omics-of-white-rot-fungus-pycnoporus-coccineus-reveals-co-regulated-cazymes-for-orchestrated-lignocellulose-breakdown
#18
Shingo Miyauchi, David Navarro, Sacha Grisel, Didier Chevret, Jean-Guy Berrin, Marie-Noelle Rosso
Innovative green technologies are of importance for converting plant wastes into renewable sources for materials, chemicals and energy. However, recycling agricultural and forestry wastes is a challenge. A solution may be found in the forest. Saprotrophic white-rot fungi are able to convert dead plants into consumable carbon sources. Specialized fungal enzymes can be utilized for breaking down hard plant biopolymers. Thus, understanding the enzymatic machineries of such fungi gives us hints for the efficient decomposition of plant materials...
2017: PloS One
https://www.readbyqxmd.com/read/28366436/fast-purification-method-of-functional-lpmos-from-streptomyces-ambofaciens-by-affinity-adsorption
#19
Susana V Valenzuela, Guillem Ferreres, Gerard Margalef, F I Javier Pastor
A simple purification method by affinity adsorption was developed to obtain functional lytic polysaccharide monooxygenases (LPMOs). The system allows the successful purification to homogeneity of the most characterized bacterial LPMO, CBP21 from Serratia marcescens, and two LPMOs from Streptomyces ambofaciens, which have not been previously characterized. The first of these new LPMOs, named SamLPMO10B is a small enzyme (15 kDa) belonging to family 10 of auxiliary activities (AA10), showing activity on β-chitin...
February 21, 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
#20
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
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