Добірка наукової літератури з теми "GH10 Xylanases"
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Статті в журналах з теми "GH10 Xylanases"
Herold, Silvia, Robert Bischof, Benjamin Metz, Bernhard Seiboth, and Christian P. Kubicek. "Xylanase Gene Transcription in Trichoderma reesei Is Triggered by Different Inducers Representing Different Hemicellulosic Pentose Polymers." Eukaryotic Cell 12, no. 3 (January 4, 2013): 390–98. http://dx.doi.org/10.1128/ec.00182-12.
Повний текст джерелаTrong Khoa, Dao, Do Thi Huyen, and Truong Nam Hai. "Probe-mining of endo-1,4-beta-xylanase from goats-rumen bacterial metagenomic DNA data." Vietnam Journal of Biotechnology 19, no. 3 (October 13, 2021): 519–28. http://dx.doi.org/10.15625/1811-4989/16632.
Повний текст джерелаMeng, Dong-Dong, Yu Ying, Xiao-Hua Chen, Ming Lu, Kang Ning, Lu-Shan Wang, and Fu-Li Li. "Distinct Roles for Carbohydrate-Binding Modules of Glycoside Hydrolase 10 (GH10) and GH11 Xylanases from Caldicellulosiruptor sp. Strain F32 in Thermostability and Catalytic Efficiency." Applied and Environmental Microbiology 81, no. 6 (January 9, 2015): 2006–14. http://dx.doi.org/10.1128/aem.03677-14.
Повний текст джерелаŠuchová, Katarína, Nikolaj Spodsberg, Kristian B. R. Mørkeberg Krogh, Peter Biely та Vladimír Puchart. "Non-Specific GH30_7 Endo-β-1,4-xylanase from Talaromyces leycettanus". Molecules 26, № 15 (30 липня 2021): 4614. http://dx.doi.org/10.3390/molecules26154614.
Повний текст джерелаNam, Gyeong-Hwa, Myoung-Uoon Jang, Min-Jeong Kim, Jung-Min Lee, Min-Jae Lee, and Tae-Jip Kim. "Enzymatic characterization of Paenibacillus amylolyticus xylanases GH10 and GH30 for xylan hydrolysis." Korean Journal of Microbiology 52, no. 4 (December 31, 2016): 463–70. http://dx.doi.org/10.7845/kjm.2016.6068.
Повний текст джерелаEmami, Kaveh, Tibor Nagy, Carlos M. G. A. Fontes, Luis M. A. Ferreira, and Harry J. Gilbert. "Evidence for Temporal Regulation of the Two Pseudomonas cellulosa Xylanases Belonging to Glycoside Hydrolase Family 11." Journal of Bacteriology 184, no. 15 (August 1, 2002): 4124–33. http://dx.doi.org/10.1128/jb.184.15.4124-4133.2002.
Повний текст джерелаLiang, Fangfang, Yi Mo, Suleman Shah, Ying Xie, Arshad Mehmood, Hesheng Jiang, and Yafen Guo. "Characterization of Two Wheat-Derived Glycoside Hydrolase Family-10 Xylanases Resistant to Xylanase Inhibitors." Journal of Food Quality 2022 (April 5, 2022): 1–10. http://dx.doi.org/10.1155/2022/9590243.
Повний текст джерелаChow, V., D. Shantharaj, Y. Guo, G. Nong, G. V. Minsavage, J. B. Jones, and J. F. Preston. "Xylan Utilization Regulon in Xanthomonas citri pv. citri Strain 306: Gene Expression and Utilization of Oligoxylosides." Applied and Environmental Microbiology 81, no. 6 (January 16, 2015): 2163–72. http://dx.doi.org/10.1128/aem.03091-14.
Повний текст джерелаYang, Jiangke, and Zhenggang Han. "Understanding the Positional Binding and Substrate Interaction of a Highly Thermostable GH10 Xylanase from Thermotoga maritima by Molecular Docking." Biomolecules 8, no. 3 (July 30, 2018): 64. http://dx.doi.org/10.3390/biom8030064.
Повний текст джерелаGhio, Silvina, Ornella Ontañon, Florencia E. Piccinni, Rubén Marrero Díaz de Villegas, Paola Talia, Daniel H. Grasso, and Eleonora Campos. "Paenibacillus sp. A59 GH10 and GH11 Extracellular Endoxylanases: Application in Biomass Bioconversion." BioEnergy Research 11, no. 1 (December 6, 2017): 174–90. http://dx.doi.org/10.1007/s12155-017-9887-7.
Повний текст джерелаДисертації з теми "GH10 Xylanases"
Wu, Haiyang. "Characterizing xylan-degrading enzymes from a putative Xylan Utilization System derived from termite gut metagenome." Thesis, Toulouse, INSA, 2018. http://www.theses.fr/2018ISAT0039.
Повний текст джерелаIn the context of bioeconomy, the discovery and study of plant-cell wall degrading enzymes is particularly relevant for the use of lignocellulosic biomass for industrial purposes. In this respect, functional metagenomics has proven to be a powerful tool to discover new enzymes from a variety of microbial ecosystems, as exemplified by work performed on the gut of the termite Pseudacanthotermes militaris. This study provided a wealth of information and identified an interesting hypothetical xylan utilization system, encoding five glycoside hydrolases (GH) and one carbohydrate esterase (CE) annotated from bacteroidales. The Pseudacanthotermes militaris-derived putative XUS cluster contains a GH10 xylanase that displays a quite complex modular arrangement wherein the GH10 catalytic module contains two insertional carbohydrate binding modules (CBM). During the preliminary work, this modular enzyme, designated Pm25, was shown to be active on xylan, thus in the present research we set out to more thoroughly characterize its biochemical and catalytic properties.The role of the CBM was also investigated, quantifying protein-carbohydrate interactions and thus providing better insight into the specific role of the modules. Taken together, the results obtained provide insight into how Pm25 modularity translates into functional properties. In second part of our study, we set out investigate the function of Pm25 in the context of the XUS cluster. To achieve this we studied a xylan utilization system, which is constituted by another GH10, GH11, GH115 and GH43. The comparison of kinetic parameters and a detailed end product analysis by mass spectrometry showed that GH10 and GH11 outweigh over 20 fold Pm25 catalytic efficiency. In parallel, we developed the use of MicroScale Thermophoresis (MST) to quantify CBM-carbohydrates interactions, an interesting approach requiring smaller concentration of proteinsand ligands compared to other biophysical methods. Overall this study highlighted the important role of Pm25 homologs in the xylan utilization system in Bacteroidetes, and pinpointed the meaning of its unusual architecture
Song, Letian. "Study and Engineering of a GH11 endo-beta-xylanase, a biomass-degrading hemicellulase." Thesis, Toulouse, INSA, 2011. http://www.theses.fr/2011ISAT0039/document.
Повний текст джерелаEngineering new and powerful enzymes for biomass hydrolysis is one area that will facilitate thefuture development of biorefining. In this respect, xylanases from family GH11 are already importantindustrial biocatalysts that can contribute to 2nd generation biorefining. The target of this study, theGH11 xylanase (Tx-Xyl) from Thermobacillus xylanilyticus is thermostable, and is thus an interestingtarget for enzyme engineering, aiming at increasing its specific activity on lignocellulosic biomass,such as wheat straw. Nevertheless, the action of xylanases on complex biomass is not yet wellunderstood, and thus the use of a rational engineering approach is not really feasible.In this doctoral study, to gain new insight into structure-function relationships, two enzymeengineering strategies have been deployed. The first concerns the development of a randommutagenesis and in vitro DNA shuffling approach, which was used in order to improve the hydrolyticpotency of Tx-Xyl on wheat straw, while the second strategy consisted in the creation of a chimericenzyme, with the aim of probing and improving -3 subsite binding, and ultimately improvinghydrolytic activity.The first key results that has been obtained is the development of a novel high-throughputscreening method, which was devised in order to reliably pinpoint mutants that can better hydrolyzewheat straw. Using this screening method, several generations of mutant libraries have beenanalyzed and a series of improved enzyme variants have been identified. One mutant, bearing silentmutations, actually leads to higher gene expression, while others have intrinsically altered catalyticproperties. Testing of mutants has shown that some of the enzyme variants can improve thesolubilization of wheat straw arabinoxylans and can work in synergy with cellulose cocktails torelease both pentose sugars and glucose.Using a semi-rational approach, 17 amino acids have been added to the N-terminal of Tx-Xyl, withthe aim of adding two extra β-strands coming from a GH11 fungal xylanase. A chimeric enzyme hasbeen successfully expressed and purified and its catalytic properties have been investigated.Although this approach has failed to create increased -3 subsite binding, the data presented revealsimportant information on structure-function relationships and suggest that Tx-Xyl may possess ahitherto unknown secondary substrate binding site. Moreover, a rational explanation for the failureof the original strategy is proposed
Molina, Gustavo Avelar. "Caracterização biofísica da dinâmica catalítica de uma xilanase GH11." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/59/59138/tde-17042016-155242/.
Повний текст джерелаThe structural dynamics underlying the function of GH11 xylanases is still unclear. New insights into the catalytic dynamics of these enzymes are crucial for engineering novel improved enzymes benefiting biotechnological and green chemistry industries. The objective of this work was to obtain new information concerning the catalytic dynamics of a GH11 xylanase, by using a combination of advanced molecular biophysics techniques, both at the bulk level and at the single molecule level (sm). Mutant GH11 xylanases from Bacillus subtilis ssp. subtilis 168 (XynA) were designed with single point cysteine mutations for labeling the residues D119 and R122 on the thumb domain, N54 on the fingers domain, and N151 on the alpha helix, followed by their construction and production by molecular biology methods. These mutants were labeled at their respective thiol groups by the polarity sensitive fluorescent probe Acrylodan, by the electron spin probe MTSSL, and by the photostable fluorescent probe AttoOxa11. The wild-type xylanase was labeled at its N-terminus by the photostable fluorescent probe Alexa Fluor® 488 5-SDP Ester. Bulk fluorescence spectrophotometry and electron paramagnetic resonance assays were used to investigate how the thumb domain dynamics of the GH11 xylanase, temperature and substrate binding were correlated. These results demonstrated that a temperature controlled, open, dynamical and flexible thumb domain state is more likely to effectively bind the substrate in a productive way, which is in complete agreement with previous studies from molecular dynamics simulations, crystallography, thermal denaturation, and function analysis by the rational design of thumb mutants for GH11 xylanases. Based on this evidence and previous studies, we proposed a hypothesis for the xylanase catalytic dynamics, focusing on the role of the thumb domain. In order to determine the xylanase affinity constant for its substrate and the relaxation times and rate constants of the thumb domain movements, fluorescence correlation spectroscopy measurements were performed. Both simple and combined measurements with photoinduced electron transfer were performed, using the xylanases labeled with photostable fluorescent probes, in the presence and absence of substrate. The results have shown longer diffusion times for the xylanases in the presence of substrate, as an effect of the enzyme affinity for it. However, it was not verified any decay curve as an effect of the dynamic suppression of the probe via PET. The same conjugates were successfully applied to fluorescence-lifetime imaging microscopy, aiming to systematically analyze the affinity for xylanase of substrates in the form of insoluble particles and films, and for water insoluble fractions from sugarcane bagasse delignification processes. In addition, the composition, structure and topology of these materials was examined. It was possible to verify the presence of xylan in most fractions of this treated bagasse, although in variable quantities
Mahanta, Pranjal. "Crystal Structure Analysis of a (B/a)8-TIM Barrel Enzyme and Its Mutants : Insights into the Role of Interactions Between Termini in Influencing Protein Stability. Experimental and Computational Study of Protein-Surface-Pockets Occluded by Tryptophan Side-Chains." Thesis, 2015. http://etd.iisc.ac.in/handle/2005/4082.
Повний текст джерелаЧастини книг з теми "GH10 Xylanases"
Qiu, Haiyan, Zhongyuan Li, Hui Wang, Shuang Li, and Tongcun Zhang. "A Novel GH10 Xylanase Xyn13-3 from Alkaline Soil: Gene Cloning and Heterogenous Expression." In Lecture Notes in Electrical Engineering, 97–103. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-4801-2_10.
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