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Related Concept Videos

Amplifying Signals via Enzymatic Cascade01:22

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Introduction to Mechanisms of Enzyme Catalysis01:13

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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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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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Catalytically Perfect Enzymes01:07

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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.
 
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Enzyme Kinetics01:19

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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.
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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.’
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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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Nanoarmored Multi-Enzyme Cascade Catalysis.

Mansi Malhotra1, Ankarao Kalluri2, Challa Vijaya Kumar3,4,5

  • 1Department of Chemistry, University of Connecticut, Storrs, CT, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 10, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed a simple, one-step method to create enhanced nano-biocatalysts using enzymes like glucose oxidase and peroxidase bound to carbon nanotubes or zirconium phosphate. These novel nano-biocatalysts show significantly improved activity and stability for cascade bio-catalysis.

Keywords:
Carbon nanotubesEnzyme assaysEnzyme kineticsEnzymologyGlucose oxidaseHorseradish peroxidaseZirconium phosphate

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Area of Science:

  • Biocatalysis and Nanomaterials Science
  • Enzyme Immobilization Techniques
  • Surface Chemistry

Background:

  • Cascade bio-catalysis often requires efficient enzyme immobilization for optimal performance.
  • Traditional methods for preparing enzyme-nanomaterial systems can be complex and multi-step.
  • Enhancing enzyme activity and stability is crucial for practical biocatalytic applications.

Purpose of the Study:

  • To report a facile single-step preparation of nanoarmored bi-enzyme systems.
  • To assemble glucose oxidase and peroxidase on 1-D (carbon nanotubes, CNT) and 2-D (α-Zirconium phosphate, α-ZrP) nanomaterials.
  • To investigate the enhanced catalytic activity and stability of these novel biocatalysts.

Main Methods:

  • Simultaneous exfoliation of bulk 1-D and 2-D nanomaterials (CNT, α-ZrP) and enzyme binding in a single step.
  • Adsorption of horseradish peroxidase (HRP), glucose oxidase (GOx), and bovine serum albumin (BSA) onto exfoliated nanomaterials.
  • Characterization using powder X-ray diffraction, electron microscopy, biochemical, and biophysical methods.

Main Results:

  • Successful preparation of nano-biocatalyst systems (GOx/HRP/BSA/CNT and GOx/HRP/BSA/α-ZrP).
  • Enzymes retained activity upon binding, with significant enhancements observed (e.g., 6-fold for CNT, 3.5-fold for α-ZrP).
  • Characterization confirmed successful enzyme binding and enhanced surface area leading to improved reagent diffusion.

Conclusions:

  • The single-step method provides a robust and efficient route to highly active and stable nano-biocatalysts.
  • Exfoliation of nanomaterials significantly boosts enzyme performance in cascade bio-catalysis.
  • These nano-biocatalyst dispersions offer a promising platform for advanced biocatalytic applications.