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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Arrhenius Plots02:34

Arrhenius Plots

The Arrhenius equation relates the activation energy and the rate constant, k, for chemical reactions. In the Arrhenius equation, k = Ae−Ea/RT, R is the ideal gas constant, which has a value of 8.314 J/mol·K, T is the temperature on the kelvin scale, Ea is the activation energy in J/mole, e is the constant 2.7183, and A is a constant called the frequency factor, which is related to the frequency of collisions and the orientation of the reacting molecules.
The Arrhenius equation can be used to...
Determination of Michaelis Constant and Maximum Elimination Rate01:20

Determination of Michaelis Constant and Maximum Elimination Rate

The Michaelis constant (KM) and the theoretical maximum process rate (Vmax) are vital parameters in the Michaelis-Menten equation, central to many biochemical reactions. They provide essential insights into enzyme kinetics and drug metabolism.
These parameters can be estimated by analyzing plasma concentration data post-drug administration. A notable example of this application is phenytoin, a drug with capacity-limited kinetics. It's recommended that phenytoin should be administered at two...
Reaction Mechanisms: The Steady-State Approximation01:26

Reaction Mechanisms: The Steady-State Approximation

The steady-state approximation, also referred to as the quasi-steady-state approximation to differentiate it from a true steady state, is a widely used method for simplifying calculations in complex reaction mechanisms. This approach is particularly useful when dealing with multi-step reactions that involve reverse reactions or several steps, which can significantly increase mathematical complexity and make the reactions nearly unsolvable analytically.The steady-state approximation operates on...
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

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Related Experiment Video

Updated: Jul 4, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

A simplified calculation method applied to enzyme inactivation during drying.

J K Liou1, K C Luyben, S Bruin

  • 1Department of Process Engineering, Agricultural University Wageningen, De Dreyen 12, 6703 BC Wageningen, the Netherlands.

Biotechnology and Bioengineering
|January 1, 1985
PubMed
Summary
This summary is machine-generated.

An approximate method accurately models drying processes with enzyme inactivation. This approach effectively predicts experimental results for soybean lipoxygenase drying in alginate gel.

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Last Updated: Jul 4, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

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Published on: January 16, 2016

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
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Published on: July 11, 2012

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Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

Area of Science:

  • Biochemical Engineering
  • Food Science
  • Chemical Engineering

Background:

  • Enzyme inactivation during drying is crucial for food preservation and process control.
  • Nonlinear diffusion models are often used to describe drying phenomena.
  • Accurate modeling of diffusion coefficients that vary with concentration is challenging.

Purpose of the Study:

  • To apply an approximate method for solving nonlinear diffusion problems.
  • To investigate simultaneous enzyme inactivation during a drying process.
  • To validate the approximate method against experimental data and numerical solutions.

Main Methods:

  • Developed and applied an approximate method for nonlinear diffusion with power-function concentration-dependent diffusion coefficients.
  • Investigated air drying of soybean lipoxygenase entrapped in a glucose calcium-alginate gel.
  • Compared experimental results with predictions from the approximate method and a numerical solution of the original model.

Main Results:

  • The approximate method showed good agreement with experimental results for soybean lipoxygenase drying.
  • Predictions from the approximate method closely matched those from the numerical solution.
  • The model effectively captures the drying behavior and enzyme inactivation.

Conclusions:

  • The approximate method provides a reliable and efficient tool for modeling drying processes with simultaneous enzyme inactivation.
  • This approach simplifies complex nonlinear diffusion problems, offering practical applications in food processing and preservation.
  • The validated method can be used for optimizing drying conditions and predicting product quality.