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Related Concept Videos

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.
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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Cofactors and Coenzymes01:24

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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
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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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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 Enzymes01:22

Introduction to Enzymes

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The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
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Enzyme Inhibition01:30

Enzyme Inhibition

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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.
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Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Multienzyme Coimmobilization on Triheterofunctional Supports.

Javier Santiago-Arcos1, Susana Velasco-Lozano1,2,3, Fernando López-Gallego1,4

  • 1Heterogeneous Biocatalysis Laboratory, CIC biomaGUNE, Edificio Empresarial "C", Paseo de Miramón 182, 20009 Donostia, Spain.

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Summary

Researchers developed a novel trifunctional support for immobilizing multiple enzymes. This method enhances enzyme stability and performance in biocatalysis, paving the way for efficient stepwise biotransformations.

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Area of Science:

  • Biocatalysis and Enzyme Immobilization
  • Applied Enzyme Engineering
  • Heterogeneous Catalysis

Background:

  • Coimmobilization of multiple enzymes on a single carrier presents significant challenges in applied biocatalysis.
  • Immobilized enzyme systems offer advantages over soluble enzymes, including enhanced stability and reusability.

Purpose of the Study:

  • To develop a versatile heterofunctional support for efficient coimmobilization of multiple enzymes.
  • To enhance the stability and catalytic performance of multienzyme systems through immobilization.

Main Methods:

  • Utilized agarose microbeads functionalized with aldehyde, amino, and cobalt chelate moieties.
  • Immobilized a multienzyme system comprising alcohol dehydrogenase, NADH oxidase, and catalase.
  • Evaluated the thermostability and catalytic performance of the immobilized system.

Main Results:

  • Achieved fast and irreversible enzyme immobilization with up to 21-fold enhancement in thermostability.
  • Demonstrated efficient coimmobilization of a three-enzyme system on the trifunctional support.
  • The confined multienzymatic system exhibited superior performance, reaching a total turnover number of 1 × 10⁵ over five cycles.

Conclusions:

  • The developed trifunctional support is a promising platform for creating robust coimmobilized multienzyme systems.
  • This approach enables enhanced catalytic efficiency for stepwise biotransformations.
  • Further applications in industrial biocatalysis are envisioned.