Academic literature on the topic 'Enzyme de modification des pectines'
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Journal articles on the topic "Enzyme de modification des pectines"
Kim, Yu-Jin, Ho Young Jeong, Seung-Yeon Kang, Jeniffer Silva, Eui-Jung Kim, Soon Ki Park, Ki-Hong Jung, and Chanhui Lee. "Physiological Importance of Pectin Modifying Genes During Rice Pollen Development." International Journal of Molecular Sciences 21, no. 14 (July 8, 2020): 4840. http://dx.doi.org/10.3390/ijms21144840.
Full textSeghini, Maria Carolina, Jacopo Tirillò, Maria Paola Bracciale, Fabienne Touchard, Laurence Chocinski-Arnault, Antonio Zuorro, Roberto Lavecchia, and Fabrizio Sarasini. "Surface Modification of Flax Yarns by Enzymatic Treatment and Their Interfacial Adhesion with Thermoset Matrices." Applied Sciences 10, no. 8 (April 23, 2020): 2910. http://dx.doi.org/10.3390/app10082910.
Full textMuñoz-Blandón, Oscar, Margarita Ramírez-Carmona, Beatriz Cuartas-Uribe, and José Antonio Mendoza-Roca. "Evaluation of Original and Enzyme-Modified Fique Fibers as an Azo Dye Biosorbent Material." Water 14, no. 7 (March 25, 2022): 1035. http://dx.doi.org/10.3390/w14071035.
Full textMorais, Patrícia Lígia Dantas de, Luiz Carlos de Oliveira Lima, Maria Raquel Alcântara de Miranda, José Donizete Alves, Ricardo Elesbão Alves, and José Daniel Silva. "Enzyme activities and pectin breakdown of sapodilla submitted to 1-methylcyclopropene." Pesquisa Agropecuária Brasileira 43, no. 1 (January 2008): 15–20. http://dx.doi.org/10.1590/s0100-204x2008000100003.
Full textShin, Yesol, Andrea Chane, Minjung Jung, and Yuree Lee. "Recent Advances in Understanding the Roles of Pectin as an Active Participant in Plant Signaling Networks." Plants 10, no. 8 (August 19, 2021): 1712. http://dx.doi.org/10.3390/plants10081712.
Full textWerchefani, Mouna, Catherine Lacoste, Hafedh Belguith, Ali Gargouri, and Chedly Bradai. "Effect of chemical and enzymatic treatments of alfa fibers on polylactic acid bio-composites properties." Journal of Composite Materials 54, no. 30 (July 13, 2020): 4959–67. http://dx.doi.org/10.1177/0021998320941579.
Full textVolchok, Anastasia, Alexandra Rozhkova, Ivan Zorov, Sergey Shcherbakov, and Arkady Sinitsyn. "Production of fruit wines using novel enzyme preparations." OENO One 49, no. 3 (September 30, 2015): 205. http://dx.doi.org/10.20870/oeno-one.2015.49.3.80.
Full textWestern, Tamara L. "Changing spaces: the Arabidopsis mucilage secretory cells as a novel system to dissect cell wall production in differentiating cellsThis review is one of a selection of papers published in the Special Issue on Plant Cell Biology." Canadian Journal of Botany 84, no. 4 (April 2006): 622–30. http://dx.doi.org/10.1139/b06-008.
Full textMATTHEW, J., S. HOWSON, M. KEENAN, and P. BELTON. "Improvement of the gelation properties of sugarbeet pectin following treatment with an enzyme preparation derived from Aspergillus niger — Comparison with a chemical modification." Carbohydrate Polymers 12, no. 3 (1990): 295–306. http://dx.doi.org/10.1016/0144-8617(90)90070-9.
Full textKim, Yang, Martin A. K. Williams, Ashley L. Galant, Gary A. Luzio, Brett J. Savary, Prasanna Vasu, and Randall G. Cameron. "Nanostructural modification of a model homogalacturonan with a novel pectin methylesterase: Effects of pH on nanostructure, enzyme mode of action and substrate functionality." Food Hydrocolloids 33, no. 1 (August 2013): 132–41. http://dx.doi.org/10.1016/j.foodhyd.2013.02.015.
Full textDissertations / Theses on the topic "Enzyme de modification des pectines"
Leschevin, Maïté. "Implication de la paroi végétale et plus particulièrement des enzymes de modification des pectines dans la tolérance au stress salin chez Arabidopsis." Thesis, Amiens, 2021. http://www.theses.fr/2021AMIE0027.
Full textSoil salinization is a alarming situation encountered in several regions of the world where the pressure on water is becoming increasingly strong, especially due to climate change and the need to increase crop yields to face a global growing population. Excess of salt in soil affects plant physiological mechanism thus reducing plant production. A better knowledge of plant defense mechanism in response to salt stress is crucial to provide efficient strategies in crop yield. The plant cell wall is the first physical barrier between the plant cell compartment and the environment and plays an essential role in cell growth and development but also in response to various stresses, including salt stress. The cell wall is a highly complex and dynamic structure, mainly composed of polysaccharides (cellulose, hemicelluloses and pectins). Pectins can be methylesterified and acetylated, and their degree of methylesterification (DM) and acetylation (DA) can be modulated in muro by specific enzymes, pectin methylesterases (PMEs, EC 3.1.1.11) and acetylesterases (PAEs, EC 3.1. 1.6). Some parcelar data from the literature showed the role of pectins and their degree of methylesterification in tolerance to salt stress. The aim of this work was to provide new insights on the role of the cell wall in response to salt stress in the glycophyte Arabidopsis thaliana. Three distinct strategies were developed. Firstly, the natural variation between two common accessions of Arabidopsis thaliana (Wassilewskija, Ws and Columbia, Col-0) in response to salt stress has been characterized using an integrative approach establishing a correlation between physiological, biochemical, metabolomics and proteomics analyses. The results showed a better tolerance to salt stress associated with the genetic background Ws with an older developmental stage, a more efficient detoxification of reactive oxygen species and a higher content of xylan, mannan and lignin within the wall. Secondly, a reverse genetics approach has been developed to determine the contribution of two pectin remodeling enzymes, AtPME3 and AtPAE7 in salt tolerance. The results showed changes in the cell wall sugar composition as a reduction in homogalacturonan and an increase in arabinan in both atpme3 and atpae7 mutants after a long exposure to salt. Additionaly, salt stress induces a modulation of the PRE activities with an alteration of the pectin methylesterification pattern indicating a role of PME and PAE in cell wall integrity under salinity. Finally, a more informative approach combining cell wall metabolism, pectin remodeling enzymes, sodium ion detoxification pathway, and impact of calcium ions on cell wall integrity was carried out to characterize the role of the cell wall in the sodium hypersensitive mutant Atsos1. The SOS1 gene encodes a Na+/H+ antiporter which is involved in Na + exclusion. Preliminary results revealed that PME and PAE activities remained unchanged in atsos1 unlike the wild-type where the activites increased. That was associated with a reduction in pectin and mannan in atsos1, which was recovered by Ca2+ supply. All these data suggest the key role of atsos1 to maintain cell wall integrity under salt stress
Turbant, Amélie. "Modification des pectines et développement de la graine d'Arabidopsis thaliana." Amiens, 2014. http://www.theses.fr/2014AMIE0115.
Full textL'Enfant, Mélanie. "Inhibition spécifique d'enzymes de modification et de dégradation des pectines." Amiens, 2014. http://www.theses.fr/2014AMIE0108.
Full textOverton, Nigel. "Enzyme catalysed modification of polymers." Thesis, Aston University, 1998. http://publications.aston.ac.uk/9608/.
Full textWindle, Claire Louise. "Altering enzyme activities using chemical modification." Thesis, University of Leeds, 2015. http://etheses.whiterose.ac.uk/11808/.
Full textO'Neil, Crystal L. "Enzyme Exploitation: Manipulating Enzyme Function for Therapy, Synthesis and Natural Product Modification." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1293722936.
Full textPirinccioglu, Necmettin. "Modification of reactivity by supramolecular complex formation." Thesis, University of Kent, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.309749.
Full textHernandez, Diana Raquel. "Regulation of Expression of a Neisseria Gonorrhoeae tRNA-Modification Enzyme (Gcp)." Diss., The University of Arizona, 2012. http://hdl.handle.net/10150/242381.
Full textOlsen, Greta A. "Characterization and modification of fluorogenic substrate coated particles for use as enzyme probes." Diss., Georgia Institute of Technology, 1999. http://hdl.handle.net/1853/27553.
Full textAydemir, Adnan [Verfasser]. "Modeling of enzyme catalyzed racemic reactions and modification of enantioselectivity / Adnan Aydemir." Hannover : Technische Informationsbibliothek und Universitätsbibliothek Hannover, 2010. http://d-nb.info/1009543792/34.
Full textBooks on the topic "Enzyme de modification des pectines"
Bearne, Stephen Lewis *. Enzyme inhibition by phosphonates and protein modification by dicarboxylic acid bis (methyl phosphates). 1991.
Find full textMortimer, Pamela. Development of an enzyme linked immunosorbent assay for the detection of hepatitis A IgG and modification of a commercial hepatitis A screening kit for avidity studies. 1995.
Find full textPuntis, John. Carbohydrate intolerance. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198759928.003.0020.
Full textThe Enzymes, Third Edition (The Enzymes). 3rd ed. Academic Press, 2001.
Find full textCooper, Bruce Andrew. Normal physiology of the renal system. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0208.
Full textBook chapters on the topic "Enzyme de modification des pectines"
Liu, Wei, and C. L. Tsou. "Kinetics of Irreversible Modification of Enzyme Activity." In Enzyme Dynamics and Regulation, 289–300. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3744-0_34.
Full textBaici, Antonio. "Dichotomous Keys to Enzyme-Modification Mechanisms." In Kinetics of Enzyme-Modifier Interactions, 463–76. Vienna: Springer Vienna, 2015. http://dx.doi.org/10.1007/978-3-7091-1402-5_10.
Full textEllis, Andrew. "Protein Modification to Meet the Demands of the Food Industry." In Industrial Enzyme Applications, 125–41. Chichester, UK: John Wiley & Sons, Ltd, 2019. http://dx.doi.org/10.1002/9783527813780.ch2_2.
Full textAra, Kazi Zubaida Gulshan, Samiullah Khan, Tejas S. Kulkarni, Tania Pozzo, and Eva Nordberg Karlsson. "Glycoside Hydrolases for Extraction and Modification of Polyphenolic Antioxidants." In Advances in Enzyme Biotechnology, 9–21. New Delhi: Springer India, 2013. http://dx.doi.org/10.1007/978-81-322-1094-8_2.
Full textSchoonen, Lise, and Jan C. M. van Hest. "Modification of CCMV Nanocages for Enzyme Encapsulation." In Methods in Molecular Biology, 69–83. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7893-9_6.
Full textChakraborty, Soma, Bishwabhusan Sahoo, Iwao Teraoka, Lisa M. Miller, and Richard A. Gross. "Enzyme-Catalyzed Regioselective Modification of Starch Nanoparticles." In ACS Symposium Series, 246–65. Washington, DC: American Chemical Society, 2005. http://dx.doi.org/10.1021/bk-2005-0900.ch017.
Full textShi, J. P., S. X. Lin, S. T. Huang, F. Miao, and Y. L. Wang. "Modification of Leucyl-tRNA Synthetase by Affinity Labeling and Limited Proteolysis." In Enzyme Dynamics and Regulation, 367–76. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3744-0_42.
Full textKruus, Kristiina, Marja-Leena Niku-Paavola, and Liisa Viikari. "Laccase — a Useful Enzyme for Modification of Biopolymers." In Biorelated Polymers, 255–61. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4757-3374-7_23.
Full textVeronese, Francesco M., Paolo Caliceti, and Oddone Schiavon. "New Synthetic Polymers for Enzyme and Liposome Modification." In ACS Symposium Series, 182–92. Washington, DC: American Chemical Society, 1997. http://dx.doi.org/10.1021/bk-1997-0680.ch013.
Full textHolzer, H. "Regulation of Enzymes by Enzyme-Catalyzed Chemical Modification." In Advances in Enzymology - and Related Areas of Molecular Biology, 297–326. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122778.ch7.
Full textConference papers on the topic "Enzyme de modification des pectines"
Xue, Yong, Shu-Bai Li, Hai-Tao Zhang, Hua-Li Nie, Li-Min Zhu, and C. Branford-White. "Enzyme Design by Chemical Modification of Papain Lysine." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162789.
Full textDjebbi, M. A., K. Charradi, A. Ben Haj Amara, and H. Ben Rhaiem. "Immobilization of LDh enzyme on Layered Double Hydroxides: Structural and morphological modification." In 2014 International Conference on Composite Materials & Renewable Energy Applications (ICCMREA). IEEE, 2014. http://dx.doi.org/10.1109/iccmrea.2014.6843803.
Full textOchi, Anna, and Hiroyuki Hori. "Complex Formations between Artificial RNA-DNA Chimera Nucleic Acids and RNA Modification Enzyme." In 2007 International Symposium on Micro-NanoMechatronics and Human Science. IEEE, 2007. http://dx.doi.org/10.1109/mhs.2007.4420836.
Full textKurimoto, Ryota, Hiroki Tsutsumi, Saki Ikeuchi, and Hiroshi Asahara. "Abstract 2370: Tumor suppression potential of tRNA modification enzyme TruBs via let-7." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2370.
Full textMatsumoto, Keisuke, Masato Abe, Yoshitaka Takano, Naoyuki Takayanagi, Yaeta Endo, and Hiroyuki Hori. "Hetero Subunits Assembly Study of RNA Modification Enzyme by Wheat Germ Cell-Free Translation System." In 2006 IEEE International Symposium on MicroNanoMechanical and Human Science. IEEE, 2006. http://dx.doi.org/10.1109/mhs.2006.320252.
Full text"Carbon Electrode based Urea Sensor - Modification of Graphite and New Polymeric Carriers for Enzyme Immobilization." In International Conference on Biomedical Electronics and Devices. SciTePress - Science and and Technology Publications, 2013. http://dx.doi.org/10.5220/0004326901970201.
Full textMazlan, Siti Zulaikha, and Sharina Abu Hanifah. "Synthesis and effect of modification on methacylate - acrylate microspheres for Trametes versicolor laccase enzyme immobilization." In THE 2014 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2014 Postgraduate Colloquium. AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4895206.
Full textBenimetskaya, L. Z., I. I. Gitelzon, Andrew L. Kozionov, S. Y. Novozhilov, V. N. Petushkov, N. S. Rodionova, and Mark I. Stockman. "Localization of the active site of an enzyme, bacterial luciferase, using two-quantum affinity modification." In Berlin - DL tentative, edited by Lars O. Svaasand. SPIE, 1991. http://dx.doi.org/10.1117/12.48227.
Full textYao, Eric, Shenshen Lai, and Jun Yan. "Abstract 3862: Empowering research on ubiquitin and ubiquitin-like protein modification cascade using recombinant enzyme systems." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3862.
Full textIntarasit, Sitthisak, Kamolchanok Umnajkitikorn, and Kobkiat Saengnil. "Nitric oxide level modification on antioxidant enzyme activity, antioxidant capacity and pericarp browning of postharvest longan fruit." In ICBBB '22: 2022 12th International Conference on Bioscience, Biochemistry and Bioinformatics. New York, NY, USA: ACM, 2022. http://dx.doi.org/10.1145/3510427.3510444.
Full textReports on the topic "Enzyme de modification des pectines"
Delmer, Deborah, Nicholas Carpita, and Abraham Marcus. Induced Plant Cell Wall Modifications: Use of Plant Cells with Altered Walls to Study Wall Structure, Growth and Potential for Genetic Modification. United States Department of Agriculture, May 1995. http://dx.doi.org/10.32747/1995.7613021.bard.
Full textDoichev, Kostadin, Veselina Georgieva, Elitsa Boteva, and Rumiana Mironova. Modification of DNA with Glucose 6-Phosphate to Examine the Glycolytic Enzyme Phosphoglucose Isomerase for DNA-amadoriase Activity. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, June 2021. http://dx.doi.org/10.7546/crabs.2021.06.06.
Full textSchaffer, Arthur, Jack Preiss, Marina Petreikov, and Ilan Levin. Increasing Starch Accumulation via Genetic Modification of the ADP-glucose Pyrophosphorylase. United States Department of Agriculture, October 2009. http://dx.doi.org/10.32747/2009.7591740.bard.
Full textLibrary, Spring. Where Does Current Quorum Sensing Research Stand. Spring Library, December 2020. http://dx.doi.org/10.47496/sl.blog.16.
Full textCohen, Jerry D., and Ephraim Epstein. Metabolism of Auxins during Fruit Development and Ripening. United States Department of Agriculture, August 1995. http://dx.doi.org/10.32747/1995.7573064.bard.
Full textRahimipour, Shai, and David Donovan. Renewable, long-term, antimicrobial surface treatments through dopamine-mediated binding of peptidoglycan hydrolases. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7597930.bard.
Full textMeiri, Noam, Michael D. Denbow, and Cynthia J. Denbow. Epigenetic Adaptation: The Regulatory Mechanisms of Hypothalamic Plasticity that Determine Stress-Response Set Point. United States Department of Agriculture, November 2013. http://dx.doi.org/10.32747/2013.7593396.bard.
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