Academic literature on the topic 'Enzyme kinetics'

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Journal articles on the topic "Enzyme kinetics"

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Guerrieri, Antonio, Rosanna Ciriello, Giuliana Bianco, Francesca De Gennaro та Silvio Frascaro. "Allosteric Enzyme-Based Biosensors—Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties". Biosensors 10, № 10 (2020): 145. http://dx.doi.org/10.3390/bios10100145.

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The present study describes the kinetics of L-lysine-α-oxidase (LO) from Trichoderma viride immobilised by co-crosslinking onto the surface of a Pt electrode. The resulting amperometric biosensor was able to analyse L-lysine, thus permitting a simple but thorough study of the kinetics of the immobilised enzyme. The kinetic study evidenced that LO behaves in an allosteric fashion and that cooperativity is strongly pH-dependent. Not less important, experimental evidence shows that cooperativity is also dependent on substrate concentration at high pH and behaves as predicted by the Monod-Wyman-Ch
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Radeef, Ziyad K. "A Comparative Analysis of Michaelis-Menten, Hill, and Allosteric Models in Drug Metabolism." Iraqi Journal of Industrial Research 12, no. 1 (2025): 98–108. https://doi.org/10.53523/ijoirvol12i1id547.

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Background: Enzyme Kinetics it is a fundamental part of metabolic biochemistry because it helps to explore the mechanism of action and interaction of all substrates under the influence as well as environmental factors. Aim: The present study intends to compare the kinetic models that have been employed to assess their efficacy in pharmaceutical kinetics and drug-trans metabolizing enzymes and efficiency. Study Design: Methodology and Experimental Design: The data were collected for separate enzymes (CYP3A4, CYP2D6 and UDP-glucuronosyltransferase) at different substrate concentrations and fit c
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Moe, Owen, and Richard Cornelius. "Enzyme kinetics." Journal of Chemical Education 65, no. 2 (1988): 137. http://dx.doi.org/10.1021/ed065p137.

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Herries, D. G. "Enzyme Kinetics." Biochemical Education 16, no. 3 (1988): 179–80. http://dx.doi.org/10.1016/0307-4412(88)90207-5.

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H.B.F.D. "Enzyme kinetics." Trends in Biochemical Sciences 13, no. 10 (1988): 411. http://dx.doi.org/10.1016/0968-0004(88)90200-9.

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WAGG, JONATHAN, and PETER H. SELLERS. "Enzyme Kinetics." Annals of the New York Academy of Sciences 779, no. 1 (1996): 272–78. http://dx.doi.org/10.1111/j.1749-6632.1996.tb44793.x.

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Lloyd, Matthew D. "Steady-state enzyme kinetics." Biochemist 43, no. 3 (2021): 40–45. http://dx.doi.org/10.1042/bio_2020_109.

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Steady-state enzyme kinetics is a cornerstone technique of biochemistry and related sciences since it allows the characterization and quantification of enzyme behaviour. Enzyme kinetics is widely used to investigate the physiological role of enzymes, determine the effects of mutations and characterize enzyme inhibitors. Well-known examples of enzyme inhibitors used to treat diseases include anti-infectives (e.g., penicillin, clavulanic acid and HIV protease inhibitors); anti-inflammatories (e.g., aspirin and ibuprofen); cholesterol-lowering statins; tyrosine kinase inhibitors used to treat can
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Markin, C. J., D. A. Mokhtari, F. Sunden, et al. "Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics." Science 373, no. 6553 (2021): eabf8761. http://dx.doi.org/10.1126/science.abf8761.

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Systematic and extensive investigation of enzymes is needed to understand their extraordinary efficiency and meet current challenges in medicine and engineering. We present HT-MEK (High-Throughput Microfluidic Enzyme Kinetics), a microfluidic platform for high-throughput expression, purification, and characterization of more than 1500 enzyme variants per experiment. For 1036 mutants of the alkaline phosphatase PafA (phosphate-irrepressible alkaline phosphatase of Flavobacterium), we performed more than 670,000 reactions and determined more than 5000 kinetic and physical constants for multiple
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Martín, J., J. Pérez-Gil, C. Acebal, and R. Arche. "Theoretical approach to the steady-state kinetics of a bi-substrate acyl-transfer enzyme reaction that follows a hydrolysable-acyl-enzyme-based mechanism. Application to the study of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lung." Biochemical Journal 266, no. 1 (1990): 47–53. http://dx.doi.org/10.1042/bj2660047.

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A kinetic model is proposed for catalysis by an enzyme that has several special characteristics: (i) it catalyses an acyl-transfer bi-substrate reaction between two identical molecules of substrate, (ii) the substrate is an amphiphilic molecule that can be present in two physical forms, namely monomers and micelles, and (iii) the reaction progresses through an acyl-enzyme-based mechanism and the covalent intermediate can react also with water to yield a secondary hydrolytic reaction. The theoretical kinetic equations for both reactions were deduced according to steady-state assumptions and the
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Meilany, Diah, Efri Mardawati, Made Tri Ari Penia Kresnowati, and Tjandra Setiadi. "KINETIC STUDY OF OIL PALM EMPTY FRUIT BUNCH ENZYMATIC HYDROLYSIS." Reaktor 17, no. 4 (2018): 197. http://dx.doi.org/10.14710/reaktor.17.4.197-202.

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As lignocellulosic biomass, Oil Palm Empty Fruit Bunch (OPEFB) can be used as the source of xylose that can be further utilized as the raw material for xylitol production. The processing of OPEFB to xylose comprises of pretreatment and hydrolysis that can be performed enzymatically. This process offers the advantages of moderate operation conditions and more environmentally friendly. This article describes the kinetic study of enzymatic hydrolysis process of OPEFB for producing xylose using self-prepared and commercial xylanase enzymes. Despite the possible mass transfer limitation, the Michae
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Dissertations / Theses on the topic "Enzyme kinetics"

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Zaman, Flora. "Kinetics of enzyme models." Thesis, University of Kent, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263701.

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Qian, Yuhui. "Study of Basic Wood Decay Mechanisms and Their Biotechnological Applications." Fogler Library, University of Maine, 2008. http://www.library.umaine.edu/theses/pdf/QianY2008.pdf.

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Moore, Robert Goodwin Douglas C. "Towards the understanding of complex biochemical systems the significance of global protein structure and thorough parametric analysis /." Auburn, Ala, 2009. http://hdl.handle.net/10415/1766.

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Ekici, Ozlem Dogan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Diss., Georgia Institute of Technology, 2003. http://hdl.handle.net/1853/5333.

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Ekici, Özlem Doğan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04062004-164633/unrestricted/ekici%5Fozlem%5Fd%5F200312%5Fphd.pdf.

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Astier, Yann. "Enzyme kinetics and electrochemical polymer transistor detection of enzyme reactions." Thesis, University of Southampton, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.273800.

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Kakkar, Tarundeep Singh. "Theoretical studies on enzyme inhibition kinetics." Diss., The University of Arizona, 1999. http://hdl.handle.net/10150/289017.

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Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interactions. To characterize the inhibitory process (competitive, non-competitive and uncompetitive) and to determine the inhibitory constant (Kᵢ), data analysis techniques (e.g., Dixon, Lineweaver-Burk, etc.) are used to linearize the inherently non-linear rate of substrate metabolism vs. substrate concentration data. These techniques were developed before the general use of computers. However, many investigators still rely on these techniques in spite of the easy availability of non-linear regression fi
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Bayram, Mustafa. "Computer algebra approaches to enzyme kinetics." Thesis, University of Bath, 1993. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.357810.

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Epstein, Todd Matthew. "Structural and kinetic studies of two enzymes catalyzing phospholipase A2 activity." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 2.39 Mb., 186 p, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3200538.

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Tenney, Joel David. "The kinetics of the chlorine dioxide generation reaction." Thesis, Georgia Institute of Technology, 1988. http://hdl.handle.net/1853/10020.

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Books on the topic "Enzyme kinetics"

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Cornish-Bowden, Athel. Enzyme kinetics. IRL Press, 1988.

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Bisswanger, Hans. Enzyme Kinetics. Wiley-VCH Verlag GmbH & Co. KGaA, 2017. http://dx.doi.org/10.1002/9783527806461.

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Alberty, Robert A. Enzyme Kinetics. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9780470940020.

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W, Wharton Christopher, ed. Enzyme kinetics. IRL Press, 1988.

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Keleti, T. Basic enzyme kinetics. Akadémiai Kiadó, 1986.

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Leskovac, Vladimir. Comprehensive enzyme kinetics. Kluwer Academic/Plenum Pub., 2003.

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Kuby, Stephen Allen. Enzyme catalysis, kinetics, and substrate binding. CRC Press, 1991.

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1930-, Cleland W. W., ed. Enzyme kinetics and mechanism. Taylor & Francis Group, 2007.

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Palfey, Bruce A., and Rebecca Switzer. Kinetics of Enzyme Catalysis. American Chemical Society, 2022. http://dx.doi.org/10.1021/acsinfocus.7e5015.

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Stein, Ross L. Kinetics of Enzyme Action. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118084410.

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Book chapters on the topic "Enzyme kinetics"

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Bagshaw, Clive R. "Enzyme Kinetics." In Biomolecular Kinetics. CRC Press, 2017. http://dx.doi.org/10.1201/9781315120355-4.

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Mc Auley, Mark Tomás. "Enzyme Kinetics." In Computer Modelling for Nutritionists. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-39994-2_3.

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Prinz, Heino. "Enzyme Kinetics." In Numerical Methods for the Life Scientist. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-20820-1_7.

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Fromm, Herbert J., and Mark S. Hargrove. "Enzyme Kinetics." In Essentials of Biochemistry. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-19624-9_5.

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Smith, C. A., and E. J. Wood. "Enzyme kinetics." In Biological Molecules. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3126-1_4.

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Dutta, Rajiv. "Enzyme Kinetics." In Fundamentals of Biochemical Engineering. Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-77901-8_2.

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De Blasio, Cataldo. "Enzyme Kinetics." In Fundamentals of Biofuels Engineering and Technology. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-11599-9_15.

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Malvis Romero, Ana, Lorenzo Pesci, Selin Kara, and Andreas Liese. "Enzyme Kinetics." In Introduction to Enzyme Technology. Springer International Publishing, 2024. http://dx.doi.org/10.1007/978-3-031-42999-6_4.

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Alberty, Robert A. "Enzyme Kinetics." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122624.ch1.

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Liu, Weijiu. "Enzyme Kinetics." In Introduction to Modeling Biological Cellular Control Systems. Springer Milan, 2012. http://dx.doi.org/10.1007/978-88-470-2490-8_2.

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Conference papers on the topic "Enzyme kinetics"

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Floros, Stylianos, Satyajeet S. Bhonsale, Sotiria Gaspari, Simen Akkermans, and Jan F. M. Van Impe. "Modelling the in vitro FooD Digestion SIMulator FooDSIM." In The 35th European Symposium on Computer Aided Process Engineering. PSE Press, 2025. https://doi.org/10.69997/sct.162389.

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Understanding the complexity of human digestion is critical for designing models that serve as valuable research tools for process simulation and prediction. Due to the high cost of medical intervention & recent advancements in in vitro digestion protocols, increased demand for inexpensive in silico solutions emerges. This study aims to develop a mathematical model that simulates the in vitro dynamic Food Digestion SIMulator (FooDSIM) functionalities via a digital twin approach. Ordinary Differential Equations (ODEs) simulate the system as a series of Continuously Stirred Tank Reactors (CS
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Tonetti, Lorenzo G., and Ruy de Sousa. "Computational Intelligence Applied to the Mathematical Modeling of the Esterification of Fatty Acids with Sugars." In The 35th European Symposium on Computer Aided Process Engineering. PSE Press, 2025. https://doi.org/10.69997/sct.190968.

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The mathematical modeling of enzymatic reactors for esterification of fatty acids with sugars in the production of biosurfactants has been a useful tool for studying and optimizing the process. In particular, artificial neural networks and fuzzy systems emerge as promising methods for developing models for those processes. In this work, regarding artificial neural networks application, coupling of networks to reactor mass balances was considered in hybrid models to infer reactant concentrations over time. Computationally, an algorithm was constructed incorporating material balances, neural rea
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Ondruch, V., J. Krejci, and D. Krejcova. "Simple Electrochemical Analysis of Enzyme Kinetics." In 2005 IEEE Engineering in Medicine and Biology 27th Annual Conference. IEEE, 2005. http://dx.doi.org/10.1109/iembs.2005.1615490.

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Vojisavljevic, V., E. Pirogova, and I. Cosic. "Influence of Electromagnetic Radiation on Enzyme Kinetics." In 2007 29th Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2007. http://dx.doi.org/10.1109/iembs.2007.4353468.

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Bashkirtseva, I., S. Zaitseva, and A. Pisarchik. "Noise-induced phantom attractor in the enzyme kinetics." In APPLICATION OF MATHEMATICS IN TECHNICAL AND NATURAL SCIENCES: 11th International Conference for Promoting the Application of Mathematics in Technical and Natural Sciences - AMiTaNS’19. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5130805.

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Lee, Alan I., and James P. Brody. "New assay for multiple single molecule enzyme kinetics." In Biomedical Optics 2005, edited by Dan V. Nicolau, Joerg Enderlein, Robert C. Leif, Daniel L. Farkas, and Ramesh Raghavachari. SPIE, 2005. http://dx.doi.org/10.1117/12.585110.

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Char, Bruce W., and Mark F. Russo. "Automatic identification of time scales in enzyme kinetics models." In the international symposium. ACM Press, 1994. http://dx.doi.org/10.1145/190347.190369.

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Uhl, Volker, Goetz Pilarczyk, and Karl-Otto Greulich. "Enzyme kinetics on a molecular level with optical microscopy." In BiOS Europe '97, edited by Irving J. Bigio, Herbert Schneckenburger, Jan Slavik, Katarina Svanberg, and Pierre M. Viallet. SPIE, 1997. http://dx.doi.org/10.1117/12.297961.

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Zhu, Linxi, Ryan Seguin, and Libin Xu. "Enzyme Kinetics of Benzalkonium Chloride Metabolism in Liver Microsomes." In ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.041.129282.

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Jin, Zhicheng, and Jesse V. Jokerst. "Understanding enzyme kinetics on coacervate as a substrate hub." In Colloidal Nanoparticles for Biomedical Applications XIX, edited by Marek Osiński and Antonios G. Kanaras. SPIE, 2024. http://dx.doi.org/10.1117/12.3005376.

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Reports on the topic "Enzyme kinetics"

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Chulalaksananukul, Warawut. Synthesis and amyl acetate by lipases from various microorgamisms. Chulalongkorn University, 1997. https://doi.org/10.58837/chula.res.1997.15.

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The main objective of this study is to synthesize biofragrance "amyl acetate" naturally extractable from the flowers of the Thai plant called "Nom Maew" (Rauwenhoffia siamenesis Scheff.) by a biotechnological method. Lipases from various microorganisms namely Aspergillus niger, Candida cylindracea, Pseudomonas species and Mucor miehei were applied to catalyze the synthetic reaction between amyl alcohol and octyl acetate through the process of "transesterification". The reaction mixture was incubated in organic solvent, hexane, at 40 ํC, with continous stirring by magnetic stirrer. The products
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Sandermann, Heinrich, Duncan Jr., and Thomas M. Lipid-Dependent Membrane Enzymes. Kinetic Modelling of the Activation of Protein Kinase C by Phosphatidylserine. Defense Technical Information Center, 1991. http://dx.doi.org/10.21236/ada302987.

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Chikwana, Vimbai. Discovery of Novel Amidotransferase Activity Involved In Archaeosine Biosynthesis and Structural and Kinetic Investigation of QueF, an Enzyme Involved in Queuosine Biosynthesis. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.140.

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Shoseyov, Oded, Steven A. Weinbaum, Raphael Goren, and Abhaya M. Dandekar. Biological Thinning of Fruit Set by RNAase in Deciduous Fruit Trees. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568110.bard.

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Fruit thinning is a common and necessary practice for commercial fruit production in many deciduous tree fruit species. Fruit thinning in apple may be accomplished with a variety of chemical thinning agents, but the use of these chemicals is a subject of environmental concern. It has been shown recently that RNase enzyme, secreted from the stigma and the style, inhibits pollen germination and pollen tube elongation. In this study we have been able to show that Aspergillus niger B-1 RNase can effectively inhibit peach and apple pollen germination, and tube elongation in-vitro, as well as thin f
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Pesis, Edna, and Mikal Saltveit. Postharvest Delay of Fruit Ripening by Metabolites of Anaerobic Respiration: Acetaldehyde and Ethanol. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7604923.bard.

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The use of pretreatments for 24 h prior to storage, under anaerobic condtions, or in the presence of the natural metabolic products, acetaldehyde (AA) and ethanol, to delay fruit ripening, was found to be effective with several climacteric fruits, among them avocado, mango, peach and tomato. The delay in ripening of avocado, peach and tomato was accompanied by inhibition of ethylene production and of fruit softening. The maintenance of fruit firmness was associated with a decrease in the activities of cell-wall-degrading enzymes, including endoglucanases (Cx), polygalacturonases (PG) and b-gal
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