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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...
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...
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...
Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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...
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...

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Related Experiment Video

Updated: Jun 26, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Understanding enzyme immobilisation.

Ulf Hanefeld1, Lucia Gardossi, Edmond Magner

  • 1Gebouw voor Scheikunde, Afdeling Biotechnologie, Technische Universiteit Delft, Julianalaan 136, Delft, 2628 BL, The Netherlands. u.hanefeld@tudelft.nl

Chemical Society Reviews
|January 27, 2009
PubMed
Summary
This summary is machine-generated.

Enzyme immobilization enhances enzyme stability and applicability in various conditions. This review explores the molecular and physical-chemical principles underlying these improvements for broader industrial and laboratory use.

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Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications
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Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications

Published on: September 23, 2013

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Related Experiment Videos

Last Updated: Jun 26, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications
14:43

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications

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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Chemical Engineering
  • Biotechnology

Background:

  • Enzymes are crucial catalysts in lab and industrial settings.
  • Enzymatic instability limits their broad application and reuse.
  • Enzyme immobilization is a key strategy to overcome instability.

Purpose of the Study:

  • To provide a comprehensive understanding of enzyme immobilization.
  • To elucidate the molecular and physical-chemical basis of immobilization benefits.
  • To guide the rational design of immobilized enzyme systems.

Main Methods:

  • Review of existing literature on enzyme immobilization techniques.
  • Analysis of reported changes in enzyme properties upon immobilization.
  • Discussion of theoretical models explaining immobilization effects.

Main Results:

  • Immobilization improves enzyme stability across diverse conditions (pH, temperature, solvents).
  • Immobilization can modify enzyme properties like substrate specificity, enantioselectivity, and reactivity.
  • The underlying molecular and physical-chemical mechanisms are often not fully understood.

Conclusions:

  • Enzyme immobilization is essential for expanding enzyme applications.
  • Further research is needed to fully understand the mechanisms driving immobilization benefits.
  • A deeper understanding will enable optimized enzyme performance in industrial processes.