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A pure, perfectly crystalline solid possessing no kinetic energy (that is, at a temperature of absolute zero, 0 K) may be described by a single microstate, as its purity, perfect crystallinity,and complete lack of motion means there is but one possible location for each identical atom or molecule comprising the crystal (W = 1). According to the Boltzmann equation, the entropy of this system is zero.
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Activity is the measure of the effective concentration of the species in solution. It can be expressed as the product of the molar concentration of the species and its activity coefficient. The activity coefficient is a dimensionless quantity and depends on the total ionic strength of the solution.
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The effective concentration of a species in a solution can be expressed precisely in terms of its activity. Activity considers the effect of electrolytes present in the vicinity of the species of interest and depends on the ionic strength of the solution. The activity of a species is expressed as the product of molar concentration and the activity coefficient of the species.
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The First Law of Thermodynamics states that energy cannot be created or destroyed, only transformed. This can be demonstrated within a classic food web where light energy from the sun is harnessed as radiant energy by plants, converted into chemical energy, and stored as complex carbohydrates. The vegetation is then consumed by animals and during the digestion process, the sugars release energy as heat. The sugars also produce chemical energy that either gets used up doing work, stored in...
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Thermodynamic Activity-Based Solvent Design for Bioreactions.

Anton Wangler1, Christoph Held1, Gabriele Sadowski1

  • 1Laboratory of Thermodynamics, Department of Biochemical and Chemical Engineering, Technische Universität (TU) Dortmund, Emil-Figge-Strasse 70, 44227 Dortmund, Germany.

Trends in Biotechnology
|June 5, 2019
PubMed
Summary
This summary is machine-generated.

This study introduces a thermodynamic activity approach to predict how cosolvents affect enzyme reactions. This method optimizes biocatalysis by improving Michaelis constants, saving time and resources.

Keywords:
Michaelis constantactivity coefficientsbiocatalysiscosolventePC-SAFTpredictions

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Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Thermodynamics

Background:

  • Enzyme-catalyzed reactions are crucial in various industrial processes.
  • Improving reaction kinetics is essential for efficiency.
  • Cosolvents are often used empirically to enhance enzyme performance.

Purpose of the Study:

  • To present a thermodynamic activity-based approach for predicting cosolvent effects on enzyme kinetics.
  • To move beyond empirical cosolvent screening in biocatalysis.
  • To optimize enzyme-catalyzed reactions for improved efficiency and reduced costs.

Main Methods:

  • Utilizing thermodynamic activity principles to model cosolvent interactions.
  • Predicting the influence of cosolvents on key enzymatic parameters, specifically Michaelis constants (Km).
  • Applying the predictive model to enhance biocatalytic process design.

Main Results:

  • Demonstrated a method to predict cosolvent impact on enzyme kinetics.
  • Showcased how thermodynamic activity can guide cosolvent selection.
  • Identified potential for significant reductions in process development time and cost.

Conclusions:

  • A thermodynamic activity-based approach offers a predictive framework for cosolvent selection in biocatalysis.
  • This strategy can significantly improve the efficiency of enzyme-catalyzed reactions.
  • The approach reduces the reliance on empirical screening, leading to cost and time savings in process optimization.