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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...
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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.
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

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Destabilization of Microtubules01:45

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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Complexation Equilibria: Factors Influencing Stability of Complexes

In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...

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Updated: Jun 8, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
08:37

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

Enzyme stabilization via cross-linked enzyme aggregates.

Munishwar N Gupta1, Smita Raghava

  • 1Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India. munishwar48@yahoo.co.uk

Methods in Molecular Biology (Clifton, N.J.)
|September 25, 2010
PubMed
Summary
This summary is machine-generated.

Cross-linked enzyme aggregates (CLEAs) offer enhanced stability and performance in various media and temperatures. These versatile biocatalysts can be engineered for multiple enzyme activities, improving their application potential.

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Area of Science:

  • Biocatalysis
  • Protein Engineering
  • Enzyme Immobilization

Background:

  • Proteins are crucial biological catalysts, but their application is often limited by stability and reusability.
  • Enzyme immobilization is a key strategy to overcome these limitations, enhancing enzyme performance and facilitating recovery.
  • Cross-linked enzyme aggregates (CLEAs) represent an advanced immobilization technique offering significant advantages.

Purpose of the Study:

  • To introduce and describe the properties of cross-linked enzyme aggregates (CLEAs).
  • To highlight the stability and performance benefits of CLEAs in diverse reaction environments.
  • To explore the potential of creating multifunctional CLEAs (combi-CLEAs) for various applications.

Main Methods:

  • Proteins are precipitated and then cross-linked using reagents like glutaraldehyde.
  • The resulting cross-linked enzyme aggregates (CLEAs) are isolated and characterized.
  • CLEAs can be prepared with single or multiple enzyme activities (combi-CLEAs).

Main Results:

  • CLEAs exhibit high stability in both aqueous and non-aqueous media.
  • CLEAs demonstrate robustness at elevated temperatures.
  • The cross-linking process influences CLEA morphology, stability, activity, and enantioselectivity.
  • Multifunctional CLEAs (combi-CLEAs) can be successfully prepared.

Conclusions:

  • Cross-linked enzyme aggregates (CLEAs) are highly stable and versatile immobilized enzyme preparations.
  • CLEAs offer superior performance in various conditions, including high temperatures and non-aqueous solvents.
  • The development of combi-CLEAs expands the utility of immobilized enzymes for complex biocatalytic processes.