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Related Concept Videos

Catalysis02:50

Catalysis

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The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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.
 
Most enzymes...
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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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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...
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Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
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Factors Influencing the Rate of Chemical Reactions01:22

Factors Influencing the Rate of Chemical Reactions

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A variety of factors influence the rate of chemical reactions. For a chemical reaction to happen, atoms must collide with enough energy to overcome the repulsion between their electrons. This energy is called activation energy. Factors influencing the rate of reaction either lower the activation energy or increase the likelihood of a successful collision.
Concentration and Pressure:
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Enzymes02:34

Enzymes

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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.
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Updated: Jun 13, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Ecofriendly approaches to efficiently enhance catalase performance.

M D Leonida1, I Kumar1, M R Elshaer1

  • 1Department of Chemistry, Biochemistry and Physics, Fairleigh Dickinson University, Teaneck, NJ 07666, USA.

International Journal of Biological Macromolecules
|September 15, 2024
PubMed
Summary

Two green methods enhance catalase (CAT) activity and stability by partially denaturing and refolding the enzyme with redox molecules. These modified enzymes show promise for biosensor applications.

Keywords:
BiosensorsCatalaseHigh hydraulic pressureIonic liquidProtein engineering

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Area of Science:

  • Biochemistry
  • Enzyme Engineering
  • Green Chemistry

Background:

  • Catalase (CAT) is crucial for antioxidant defense.
  • Enhancing enzyme stability and activity is vital for industrial applications.
  • Green chemistry approaches minimize environmental impact.

Purpose of the Study:

  • To develop two novel, green methods for enhancing catalase activity and stability.
  • To compare the efficacy of ionic liquid and high hydraulic pressure treatments.
  • To investigate the potential of modified catalase in biosensor development.

Main Methods:

  • Enzyme modification via transient ionic liquid (IL) exposure with redox molecules.
  • Enzyme modification via high hydraulic pressure (HHP) treatment with redox molecules (reagentless).
  • Dialysis for refolding and redox molecule entrapment, creating "wired" enzymes.
  • Construction and testing of enzyme electrodes for hydrogen peroxide detection.

Main Results:

  • Both IL and HHP methods successfully enhanced CAT activity and stability.
  • Modified CAT retained catalytic effect and exhibited linear behavior in biosensors.
  • The HHP method offers a reagentless approach to enzyme modification.
  • Comparative analysis of parameters, residual activity, and redox molecule interactions was performed.

Conclusions:

  • Simple, green processes can significantly enhance catalase performance.
  • Modified catalase demonstrates potential for amperometric biosensors.
  • Applications are foreseen in the food, pharmaceutical, and textile industries.