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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...
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.
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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.
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...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Modifying enzyme activity and selectivity by immobilization.

Rafael C Rodrigues1, Claudia Ortiz, Ángel Berenguer-Murcia

  • 1Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil.

Chemical Society Reviews
|October 13, 2012
PubMed
Summary
This summary is machine-generated.

Enzyme immobilization can alter enzyme properties, sometimes enhancing activity, specificity, and selectivity. This review explores reasons for improved enzyme performance after immobilization, including structural changes and altered microenvironments.

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Area of Science:

  • Biocatalysis
  • Enzyme Engineering
  • Biotechnology

Background:

  • Enzyme immobilization can lead to changes in enzyme activity, specificity, and selectivity.
  • While immobilization often results in decreased enzyme properties due to support interactions, it can also enhance them.
  • These alterations are frequently linked to modifications in the enzyme's structure.

Purpose of the Study:

  • To review the mechanisms behind enhanced enzyme activity, specificity, and selectivity upon immobilization.
  • To explain how immobilization can lead to improvements, both real and apparent, in enzyme performance.
  • To highlight the potential of creating diverse immobilized enzyme libraries for discovering superior biocatalysts.

Main Methods:

  • Literature review of studies on enzyme immobilization and its effects on enzyme properties.
  • Analysis of structural and non-structural factors influencing immobilized enzyme behavior.
  • Discussion of phenomena like interfacial activation, enzyme rigidification, and microenvironmental effects (e.g., gradients, partitioning, inhibition blocking).

Main Results:

  • Immobilization can stabilize hyperactivated enzyme forms (e.g., lipases on hydrophobic supports).
  • Preventing enzyme aggregation and increasing rigidity under harsh conditions preserves or enhances activity.
  • Non-structural factors such as diffusional limitations and altered partitioning can significantly improve enzyme performance.

Conclusions:

  • Enzyme immobilization offers various strategies to enhance biocatalyst performance.
  • Understanding the interplay between structural changes and microenvironmental effects is crucial for optimizing immobilized enzymes.
  • Developing broad libraries of immobilized enzymes is key to identifying biocatalysts with superior properties compared to their free counterparts.