Contributors to this volume explore how Asian influences have been adapted to American desires in literary works and at Buddhist poetics, or how Buddhist practices emerge in literary works. Starting with early aesthetic theories of Ernest Fenollosa, made famous but also distorted by Ezra Pound, the book moves on to the countercultural voices associated with the Beat movement and its friends and heirs such as Ginsberg, Kerouac, Snyder, Giorno, Waldman, and Whalen.
Received Feb 8; Accepted Mar Abstract A new method for determination of the optimum temperature and activation energies based on an idea of the average rate of enzymatic reaction has been developed. A mathematical model describing the effect of temperature on a dimensionless activity for enzyme deactivation following the first-order kinetics has been derived.
The necessary condition for existence of the function extreme of the optimal temperature has been applied in the model. The developed method has been verified using the experimental data for inulinase from Kluyveromyces marxianus.
Optimum temperature, Biokinetics, Enzyme activity, Enzyme deactivation, Kinetic parameters, Inulinase Introduction Determination of optimum temperature is commonly applied to characterize enzymes.
Both the rate of chemical reaction, as well as the rate of enzyme deactivation, increase with increasing temperature.
At moderate temperatures deactivation rate is negligible and can be ignored, while the rate of enzymatic reaction increases with temperature, as for any chemical reaction. At higher temperatures the effect of enzyme deactivation on its final activity increases.
When the reaction occurs at an optimum temperature, equilibrium between these two processes is established. Some authors [ 5 — 7 ] demonstrate a relationship between the activity and temperature on Arrhenius diagram, and the intersection point of straight lines determines optimum temperature. Such determined optimum temperature has, however, limited significance since it depends upon assay duration.
With increased time of assay the optimum is shifted toward lower temperatures.
However, it is possible to make use of the optimum temperature for qualitative comparison of stability of enzymes from various sources, if such measurements have been carried out under identical conditions substrate type and concentration, pH, etc.
Application of optimal temperature control in a batch bioreactor enables significant reduction of the reaction time [ 8 ], or the amount of the spent enzyme [ 9 ], when compared to an isothermal process.
The advantages resulting from implementation of the optimal temperature control are the greater the higher is the value of the quotient of activation energy for enzyme deactivation process and that of reaction activation.
The activation energies indispensable for optimization computations are determined experimentally or calculated from the activity graph. However, accounting for experimental data in the vicinity extreme of the enzyme activity leads to considerable errors in estimating activation energies.
In modeling thermal stability and activity of inulinase Santos et al. In this concept kinetic parameters are related to the reaction rate at a fixed moment of the measurement, though due to enzyme deactivation gradual decrease of the reaction rate takes place, so in fact an average value of this rate is determined.
The method of Santos et al. The aim of the present work was to develop a mathematical model that would take into account the effects of time and temperature on enzyme activity determined using the concept of the average reaction rate.
The model will be verified by means of the experimental data for inulinase [ 1015 ]. Theory During determination of the enzyme activity the experimental conditions are selected in such a way, that the effects of the substrate and product concentrations variations can be neglected.Published: Mon, 5 Dec In the most industrial countries, the competitive markets are rarely free from government intervention.
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Introduction. In this experiment, you will observe the reaction between crystal violet . Additionally by performing essentially the same experiments but with temperature changes one can determine how k is affected by temperature changes and the new activation energy.
Also, from graphs the activation energy was determined to be kJ/mol. INTRODUCTION: The rate of a chemical reaction often depends. More molecules have enough energy that many more collisions have the necessary activation energy.
Raises reaction rate a great deal. (c) Catalytic nickel lowers the activation energy needed for a reaction. Essay Nacl Affects on Enzymatic Reaction. Concentration Had on the Rate of Reaction of Catecholase Enzymes in a Potato (Solanum tuberosum).
Abstract Enzymes are a key component of a cell. They make chemical reactions happen faster because they lower the .