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Related Concept Videos

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...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
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...
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...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...

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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

Diffusion and the limiting substrate in two-substrate immobilized enzyme systems.

J K Leypoldt1, D A Gough

  • 1Department of Applied Mechanics and Engineering Sciences, Bioengineering Group, University of California, San Diego, La Jolla, California 92093, USA.

Biotechnology and Bioengineering
|December 1, 1982
PubMed
Summary
This summary is machine-generated.

Mass transport resistances significantly impact immobilized enzyme systems. The limiting substrate, crucial for reaction rates, can change due to combined internal and external transport effects, especially under high resistance conditions.

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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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Defining Substrate Specificities for Lipase and Phospholipase Candidates

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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

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Last 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

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
10:45

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Biotechnology

Background:

  • Immobilized enzyme systems are crucial for biocatalysis and biosensing.
  • Mass transport limitations can significantly affect the efficiency of these systems.
  • Understanding substrate transport is key to optimizing enzyme reactor design.

Purpose of the Study:

  • To theoretically investigate the influence of mass transport resistances on two-substrate immobilized enzyme systems.
  • To identify the factors determining substrate limitation in such systems.
  • To explore implications for enzyme electrode and chemical reactor design.

Main Methods:

  • Theoretical analysis of mass transport phenomena.
  • Modeling of reaction kinetics in immobilized enzyme systems.
  • Investigation of substrate diffusion and concentration gradients within the support matrix.

Main Results:

  • Mass transport resistances primarily affect the overall reaction rate through the transport of the limiting substrate.
  • In the absence of external resistances, substrate limitation is predictable by concentration ratios, substrate permeabilities, and stoichiometry.
  • Combined internal and external mass transport resistances can lead to the other substrate becoming limiting, particularly at high resistance values.

Conclusions:

  • The interplay between internal and external mass transport is critical in determining substrate limitation in two-substrate immobilized enzyme systems.
  • High mass transport resistances necessitate careful consideration of substrate diffusion in system design.
  • These findings have direct applications in optimizing the performance of enzyme electrodes and chemical reactors.