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Relevant bibliographies by topics / Enzyme kinetics

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Academic literature on the topic 'Enzyme kinetics'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 August 2024

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Journal articles on the topic "Enzyme kinetics"

1

Guerrieri, Antonio, Rosanna Ciriello, Giuliana Bianco, Francesca De Gennaro, and Silvio Frascaro. "Allosteric Enzyme-Based Biosensors—Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties." Biosensors 10, no. 10 (October 17, 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-Changeux model for allosteric enzymes. According to this model, the existence of two different conformational states of the enzyme was postulated, which differ in Lys species landing on LO to form the enzyme–substrate complex. Considerations about the influence of the peculiar LO kinetics on biosensor operations and extracorporeal reactor devices will be discussed as well. Not less important, the present study also shows the effectiveness of using immobilised enzymes and amperometric biosensors not only for substrate analysis, but also as a convenient tool for enzyme kinetic studies.

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Moe, Owen, and Richard Cornelius. "Enzyme kinetics." Journal of Chemical Education 65, no. 2 (February 1988): 137. http://dx.doi.org/10.1021/ed065p137.

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Herries, D. G. "Enzyme Kinetics." Biochemical Education 16, no. 3 (July 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 (October 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 (April 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 (May 10, 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 cancer; and Viagra. Commonly, new disease treatments are discovered by using enzyme kinetics to identify the few active compounds residing within a large compound collection (‘high-throughput screening’). The subject of enzyme kinetics is typically introduced to first-year undergraduates with a mathematical description of behaviour. This Beginners Guide will give a brief overview of experimental enzyme kinetics and the characterization of enzyme inhibitors. Colorimetric assays using a microtitre plate will be considered, although most principles also apply to other assays.

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Markin, C. J., D. A. Mokhtari, F. Sunden, M. J. Appel, E. Akiva, S. A. Longwell, C. Sabatti, D. Herschlag, and P. M. Fordyce. "Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics." Science 373, no. 6553 (July 22, 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 substrates and inhibitors. We uncovered extensive kinetic partitioning to a misfolded state and isolated catalytic effects, revealing spatially contiguous regions of residues linked to particular aspects of function. Regions included active-site proximal residues but extended to the enzyme surface, providing a map of underlying architecture not possible to derive from existing approaches. HT-MEK has applications that range from understanding molecular mechanisms to medicine, engineering, and design.

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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 (February 15, 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 theoretical plots were predicted. The experimental kinetics of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lung fitted the proposed equations with great accuracy. Also, kinetics of inhibition by products behaved as expected. It was concluded that the competition between two nucleophiles for the covalent acyl-enzyme intermediate, and not a different enzyme action depending on the physical state of the substrate, is responsible for the differences in kinetic pattern for the two activities of the enzyme. This conclusion, together with the fact that the kinetic equation for the transacylation is quadratic, generates a ‘hysteretic’ pattern that can provide the basis of self-regulatory properties for enzymes to which this model could be applied.

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WU, Jia-Wei, Zhi-Xin WANG, and Jun-Mei ZHOU. "Inactivation kinetics of dihydrofolate reductase from Chinese hamster during urea denaturation." Biochemical Journal 324, no. 2 (June 1, 1997): 395–401. http://dx.doi.org/10.1042/bj3240395.

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The kinetic theory of substrate reaction during modification of enzyme activity has been applied to the study of inactivation kinetics of Chinese hamster dihydrofolate reductase by urea [Tsou (1988) Adv. Enzymol. Relat. Areas Mol. Biol. 61, 381–436]. On the basis of the kinetic equation of substrate reaction in the presence of urea, all microscopic kinetic constants for the free enzyme and enzyme–substrate binary and ternary complexes have been determined. The results of the present study indicate that the denaturation of dihydrofolate reductase by urea follows single-phase kinetics, and changes in enzyme activity and tertiary structure proceed simultaneously in the unfolding process. Both substrates, NADPH and 7,8-dihydrofolate, protect dihydrofolate reductase against inactivation, and enzyme–substrate complexes lose their activity less rapidly than the free enzyme.

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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 (February 2, 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 Michaelis Menten kinetics was hypothesized. The results indicated that the reaction at pH 5 and 60°C followed the Michaelis Menten kinetics, with Vm of 0.84 g/L-h and Km of 48.5 g/L for the commercial enzyme, and Vm of 0,38 g/L-h and Km of 0,37 g/L for the self-prepared enzyme. The reaction is affected by temperature, with Ea of 8.6 kcal/gmol. The performance of self-prepared xylanase enzyme was not yet as good as the commercial enzyme, Cellic Htec 2. Keywords: enzymatic hydrolysis; kinetics parameter; OPEFB; xylanase; xylose

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Dissertations / Theses on the topic "Enzyme kinetics"

1

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 fitting programs. In Chapter 2, three methods (simultaneous nonlinear regression fit (SNLR); Dixon; non-simultaneous, nonlinear fit [K(m,app)]) were compared for estimating Ki from simulated data sets generated from a competitive inhibition model equation with 10% CV added random error to the data values. Of the three methods, the SNLR method was found to be the most robust, the fastest and easiest to implement. The K(m,app) method also gave good estimates but was more time-consuming. The Dixon method failed to give accurate and precise estimates of Kᵢ. The purpose of the study in Chapter 3 was to examine the minimal experimental design needed to obtain reliable and robust estimates of Kᵢ (as well as V(max) and K(m)). Four cases were examined. In the experimental design that relied upon the least amount of data, a control data set was fit simultaneously with one of the substrate-inhibitor pairs (25-10 or 250-100 μM). A total of 4 rate values were analyzed per fit (i.e., 3 control + 1 inhibitor value). A total of 100 data sets were fit per substrate-inhibitor pair. The preceding was repeated for a random error of 20 %CV. Thus, the total number of experiments was reduced from 108 (in Chapter 2) to 12 (in Chapter 3) (Case IV). Good estimates of the enzyme kinetic parameters were obtained. In Chapter 4, the ability of the SNLR method to identify the correct mechanism of inhibition was evaluated; competitive or noncompetitive enzyme-inhibition. Two experimental designs were examined ("conventional, non-optimal" and "semi-minimal"). The semi-minimal design was successful in discriminating between the two enzyme-inhibition mechanisms even for data with 30 %CV added random error.

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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"

1

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

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

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

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

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5

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

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6

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

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7

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

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

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9

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

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

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Book chapters on the topic "Enzyme kinetics"

1

Bagshaw, Clive R. "Enzyme Kinetics." In Biomolecular Kinetics, 89–114. Boca Raton : Taylor & Francis/CRC Press, 2017. | Series: Foundations of biochemistry and biophysics |: 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, 31–40. Cham: 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, 97–118. Berlin, Heidelberg: 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, 81–122. Berlin, Heidelberg: 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, 83–104. Dordrecht: 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, 8–49. Berlin, Heidelberg: 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, 209–20. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-11599-9_15.

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Alberty, Robert A. "Enzyme Kinetics." In Advances in Enzymology - and Related Areas of Molecular Biology, 1–64. Hoboken, NJ, USA: 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, 11–36. Milano: Springer Milan, 2012. http://dx.doi.org/10.1007/978-88-470-2490-8_2.

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Gardner, Aaron, Wilko Duprez, Sarah Stauffer, Dewi Ayu Kencana Ungu, and Frederik Clauson-Kaas. "Enzyme Kinetics." In Labster Virtual Lab Experiments: Basic Biochemistry, 57–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-58499-6_4.

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Conference papers on the topic "Enzyme kinetics"

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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. New York, New York, USA: 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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Robinson, Tom, Hugh B. Manning, Christopher Dunsby, Mark A. A. Neil, Geoff S. Baldwin, Andrew J. de Mello, and Paul M. W. French. "Investigating fast enzyme-DNA kinetics using multidimensional fluorescence imaging and microfluidics." In MOEMS-MEMS, edited by Holger Becker and Wanjun Wang. SPIE, 2010. http://dx.doi.org/10.1117/12.840035.

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FENG, Y., R. H. DAVIES, and J. D. ANDRADE. "ENZYME KINETICS MODEL OF THE BACTERIAL LUCIFERASE REACTIONS FOR BIOSENSOR APPLICATIONS." In Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0100.

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Reports on the topic "Enzyme kinetics"

1

Sandermann, Heinrich, Duncan Jr., and Thomas M. Lipid-Dependent Membrane Enzymes. Kinetic Modelling of the Activation of Protein Kinase C by Phosphatidylserine. Fort Belvoir, VA: Defense Technical Information Center, January 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, January 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, August 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 fruit in peach and apple, and reduce the number of seeds in citrus. The objectives of the research were to detrmine the conditions for effective thinning of (USA and Israel), develop fermentation process for cost effective production of RNase from A. niger. (Israel), and clone apple S-RNase cDNA (USA). All the objectives of the research were addressed. We have determined the optimal fermentation conditions for cost effective production of the A. niger at a 20,000 liters scale. TheA. niger B1 RNase was isolated to homogeneity and its kinetic and biochemical properties including its N-terminal sequence were fully characterized. The field test results both in Israel and California have shown variability in effectiveness and more work is needed to define the RNase concentration necessary to completely inhibit pollen development. Plant transformation vectors expressing anti-sense apple S-RNase genes were constructed (USA) with an attempt to produce self compatible transgenic apple trees. Bovine S-Protein cDNA was cloned and successfully expressed in E. coli (Israel). Plant transformation vector expressing the S-Protein gene was constructed (USA) with an attempt to produce transgenic plants expressing S-protein in the style. Exogenous application of S-peptide to these plants will result in active RNase and consequently prevention of fertilization.

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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, October 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-galactosidases. In peaches the AA- and N2-treated fruits were firmer after 3 weeks storage and contained higher amount of insoluble pectin than untreated controls. We showed that AA vapors are able to inhibit ripening, ethylene production and ethylene induction in the presence of 1-amino-cyclopropane-1-carboxylic acid (ADD) in avocado and mango tissue. Ethylene induced by ACC is taken as an indicator of ACC oxidase activity. ACC oxidase activity in AA-treated avocado fruit was much lower than in the untreated fruit. In carnation flowers very little ethylene was produced by ethanol-treated flowers, and the normal increases in ACC content and ACC oxidase activity were also suppressed. Using kinetic studies and inhibitors of alcohol dehydrogenase (ADH), we showed that AA, not ethanol, was the active molecule in inhibiting ripening of tomato fruit. Application of anaerobiosis or anaerobic metabolites was effective in reduction of chilling injury (CI) in various plant tissues. Pretreatment with a low-O2 atmosphere reduced CI symptoms in avocado; this effect was associated with higher content of the free sylfhydryl (SH) group, and induction of the detoxification enzymes, catalase and peroxidase. Application of AA maintained firmer and brighter pulp tissue (non-oxidative), which was associated with higher free SH content, lower ethylene and ACC oxidase activities, and higher activities of catalase and peroxidase. Ethanol was found to reduce CI in other plant tissue. In roots of 24-h-old germinated cucumber seeds, exposure to 0.4-M ethanol shock for 4 h reduced chilling-induced ion leakage. In cucumber cotyledons it appears that alcohols may reduce CI by inducing stomata closure. In cotyledon discs held in N2 at 10C for 1 day, there accumulated sufficient endogenously synthesized ethanol to confer tolerance to chilling at 2.5C for 5 days.

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