Relevant bibliographies by topics / Biomass degrading enzymes

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Academic literature on the topic 'Biomass degrading enzymes'

Author: Grafiati
Published: 4 June 2021
Last updated: 3 February 2022

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Journal articles on the topic "Biomass degrading enzymes"

1

Lunin, Vladimir, Markus Alahuhta, Gregg Beckham, et al. "Structural studies of biomass degrading enzyme systems." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1812. http://dx.doi.org/10.1107/s2053273314081881.

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Renewable energy today comprises wind, photovoltaics, geothermal, and biofuels. Biomass is the leading source of renewable, sustainable energy used for the production of liquid transportation fuels. While the focus is shifting today from the ethanol towards next generation or advanced biofuels the real challenge however remains the same: reducing the recalcitrance of biomass to deconstruction, which yields the sugars needed for further processing. NREL's Biosciences Center conducts studies of the fundamental nature of the plant cell wall; as well as those enzyme systems utilized in Nature to deconstruct it. These systems could be classified in two ways: the "free enzymes" and the "cellulosomes." Cellulosomes are self-assembling, multi-enzyme machinery that can include dozens and hundreds of catalytic domains and cellulose binding modules interconnected by linker peptides. We will present a structural overview of the biomass degrading enzymes from fungi using Trichoderma reesei and Penicillum funiculosum as examples. The bacterial cellulosome system discussed will be from a thermophile Clostridium thermocellum and bacterial free enzyme example will be the hyperthermophile, Caldicellulosiruptor bescii. To study these systems, we combined classical biochemistry and molecular biology, mass spectrometry, electron microscopy, high throughput robotics, macromolecular crystallography, and molecular dynamics. We seek to understand the properties and structure of biomass and plant cell walls, the structure-function relationships of the relevant hydrolytic enzymes, and the ways these enzymes interact with and alter the biomass during the degradation. Thorough understanding of the details of the molecular machinery at work has led to the development of improved enzyme cocktails that have reduced the cost of biomass conversion to renewable fuels so that today, this technology is becoming competitive with traditional fossil fuels.
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2

Lee, Charles C. "Screening assays for biomass-degrading enzymes." Biofuels 1, no. 4 (2010): 575–88. http://dx.doi.org/10.4155/bfs.10.26.

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3

Frandsen, Kristian E. H., Tobias Tandrup, Jens-Christian N. Poulsen, et al. "Active site evolution in biomass degrading enzymes." Acta Crystallographica Section A Foundations and Advances 75, a2 (2019): e124-e124. http://dx.doi.org/10.1107/s2053273319094324.

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4

Saini, Anita, Neeraj K. Aggarwal, Anuja Sharma, and Anita Yadav. "Actinomycetes: A Source of Lignocellulolytic Enzymes." Enzyme Research 2015 (December 17, 2015): 1–15. http://dx.doi.org/10.1155/2015/279381.

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Lignocellulose is the most abundant biomass on earth. Agricultural, forest, and agroindustrial activities generate tons of lignocellulosic wastes annually, which present readily procurable, economically affordable, and renewable feedstock for various lignocelluloses based applications. Lignocelluloses are the focus of present decade researchers globally, in an attempt to develop technologies based on natural biomass for reducing dependence on expensive and exhaustible substrates. Lignocellulolytic enzymes, that is, cellulases, hemicellulases, and lignolytic enzymes, play very important role in the processing of lignocelluloses which is prerequisite for their utilization in various processes. These enzymes are obtained from microorganisms distributed in both prokaryotic and eukaryotic domains including bacteria, fungi, and actinomycetes. Actinomycetes are an attractive microbial group for production of lignocellulose degrading enzymes. Various studies have evaluated the lignocellulose degrading ability of actinomycetes, which can be potentially implemented in the production of different value added products. This paper is an overview of the diversity of cellulolytic, hemicellulolytic, and lignolytic actinomycetes along with brief discussion of their hydrolytic enzyme systems involved in biomass modification.
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Agrawal, Ruchi, Ruchi Gaur, Anshu Mathur, et al. "Improved saccharification of pilot-scale acid pretreated wheat straw by exploiting the synergistic behavior of lignocellulose degrading enzymes." RSC Advances 5, no. 87 (2015): 71462–71. http://dx.doi.org/10.1039/c5ra13360b.

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6

Book, Adam J., Gina R. Lewin, Bradon R. McDonald, et al. "Cellulolytic Streptomyces Strains Associated with Herbivorous Insects Share a Phylogenetically Linked Capacity To Degrade Lignocellulose." Applied and Environmental Microbiology 80, no. 15 (2014): 4692–701. http://dx.doi.org/10.1128/aem.01133-14.

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ABSTRACTActinobacteria in the genusStreptomycesare critical players in microbial communities that decompose complex carbohydrates in the soil, and these bacteria have recently been implicated in the deconstruction of plant polysaccharides for some herbivorous insects. Despite the importance ofStreptomycesto carbon cycling, the extent of their plant biomass-degrading ability remains largely unknown. In this study, we compared four strains ofStreptomycesisolated from insect herbivores that attack pine trees: DpondAA-B6 (SDPB6) from the mountain pine beetle, SPB74 from the southern pine beetle, and SirexAA-E (SACTE) and SirexAA-G from the woodwasp,Sirex noctilio. Biochemical analysis of secreted enzymes demonstrated that only two of these strains, SACTE and SDPB6, were efficient at degrading plant biomass. Genomic analyses indicated that SACTE and SDPB6 are closely related and that they share similar compositions of carbohydrate-active enzymes. Genome-wide proteomic and transcriptomic analyses revealed that the major exocellulases (GH6 and GH48), lytic polysaccharide monooxygenases (AA10), and mannanases (GH5) were conserved and secreted by both organisms, while the secreted endocellulases (GH5 and GH9 versus GH9 and GH12) were from diverged enzyme families. Together, these data identify two phylogenetically related insect-associatedStreptomycesstrains with high biomass-degrading activity and characterize key enzymatic similarities and differences used by these organisms to deconstruct plant biomass.
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7

Wu, Vincent W., Nils Thieme, Lori B. Huberman, et al. "The regulatory and transcriptional landscape associated with carbon utilization in a filamentous fungus." Proceedings of the National Academy of Sciences 117, no. 11 (2020): 6003–13. http://dx.doi.org/10.1073/pnas.1915611117.

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Filamentous fungi, such asNeurospora crassa, are very efficient in deconstructing plant biomass by the secretion of an arsenal of plant cell wall-degrading enzymes, by remodeling metabolism to accommodate production of secreted enzymes, and by enabling transport and intracellular utilization of plant biomass components. Although a number of enzymes and transcriptional regulators involved in plant biomass utilization have been identified, how filamentous fungi sense and integrate nutritional information encoded in the plant cell wall into a regulatory hierarchy for optimal utilization of complex carbon sources is not understood. Here, we performed transcriptional profiling ofN. crassaon 40 different carbon sources, including plant biomass, to provide data on how fungi sense simple to complex carbohydrates. From these data, we identified regulatory factors inN. crassaand characterized one (PDR-2) associated with pectin utilization and one with pectin/hemicellulose utilization (ARA-1). Using in vitro DNA affinity purification sequencing (DAP-seq), we identified direct targets of transcription factors involved in regulating genes encoding plant cell wall-degrading enzymes. In particular, our data clarified the role of the transcription factor VIB-1 in the regulation of genes encoding plant cell wall-degrading enzymes and nutrient scavenging and revealed a major role of the carbon catabolite repressor CRE-1 in regulating the expression of major facilitator transporter genes. These data contribute to a more complete understanding of cross talk between transcription factors and their target genes, which are involved in regulating nutrient sensing and plant biomass utilization on a global level.
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8

Patyshakuliyeva, Aleksandrina, Daniel L. Falkoski, Ad Wiebenga, Klaas Timmermans, and Ronald P. de Vries. "Macroalgae Derived Fungi Have High Abilities to Degrade Algal Polymers." Microorganisms 8, no. 1 (2019): 52. http://dx.doi.org/10.3390/microorganisms8010052.

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Marine fungi associated with macroalgae are an ecologically important group that have a strong potential for industrial applications. In this study, twenty-two marine fungi isolated from the brown seaweed Fucus sp. were examined for their abilities to produce algal and plant biomass degrading enzymes. Growth of these isolates on brown and green algal biomass revealed a good growth, but no preference for any specific algae. Based on the analysis of enzymatic activities, macroalgae derived fungi were able to produce algae specific and (hemi-)cellulose degrading enzymes both on algal and plant biomass. However, the production of algae specific activities was lower than the production of cellulases and xylanases. These data revealed the presence of different enzymatic approaches for the degradation of algal biomass by macroalgae derived fungi. In addition, the results of the present study indicate our poor understanding of the enzymes involved in algal biomass degradation and the mechanisms of algal carbon source utilization by marine derived fungi.
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9

Bissaro, Bastien, Zarah Forsberg, Yan Ni, Frank Hollmann, Gustav Vaaje-Kolstad, and Vincent G. H. Eijsink. "Fueling biomass-degrading oxidative enzymes by light-driven water oxidation." Green Chemistry 18, no. 19 (2016): 5357–66. http://dx.doi.org/10.1039/c6gc01666a.

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10

Henske, John K., Sean P. Gilmore, Charles H. Haitjema, Kevin V. Solomon, and Michelle A. O'Malley. "Biomass-degrading enzymes are catabolite repressed in anaerobic gut fungi." AIChE Journal 64, no. 12 (2018): 4263–70. http://dx.doi.org/10.1002/aic.16395.

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