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Related Concept Videos

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.
 
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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

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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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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 Enzymes01:22

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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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Introduction to Enzyme Kinetics01:19

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Coprecipitated Enzyme-Encapsulated Covalent Organic Frameworks for Biocatalysis.

Satyadip Paul1, Mani Gupta2, Shayan Karak1

  • 1Department of Chemical Sciences, Indian Institute of Science Education and Research, Mohanpur, Kolkata 741246, India.

Journal of the American Chemical Society
|June 27, 2025
PubMed
Summary
This summary is machine-generated.

We developed a one-pot synthesis to encapsulate enzymes in covalent organic frameworks (COFs), enhancing their stability and reusability. This method improves enzyme performance under harsh conditions, enabling broader biocatalysis applications.

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Area of Science:

  • Biocatalysis
  • Materials Science
  • Nanotechnology

Background:

  • Enzymes are efficient biocatalysts but exhibit limited stability under harsh industrial conditions.
  • Developing robust enzyme immobilization strategies is crucial for expanding their practical applications.
  • Covalent organic frameworks (COFs) offer a promising platform for biomolecule encapsulation due to their tunable structures and high surface areas.

Purpose of the Study:

  • To develop a facile aqueous synthesis for enzyme-encapsulated COFs.
  • To investigate the interactions between encapsulated enzymes and the COF matrix.
  • To evaluate the enhanced stability and reusability of encapsulated enzymes.

Main Methods:

  • One-pot aqueous synthesis of TpAzo COFs encapsulating various enzymes, including beta-glucosidase (BGL) and alkaline phosphatase (ALP).
  • Solid-state 2D NMR correlation spectroscopy to probe enzyme-COF interactions at the molecular level.
  • Scattering-type scanning near-field optical microscopy (s-SNOM) and nanoscale Fourier-transform infrared spectroscopy (nanoFTIR) for validation.
  • Assays to measure enzyme activity, stability under denaturing conditions (SDS), and recyclability.

Main Results:

  • Successful encapsulation of multiple enzymes and proteins within the TpAzo COF.
  • Direct evidence of molecular interactions between enzymes and the COF backbone, confirming structural integrity.
  • Encapsulated BGL and ALP retained high catalytic activity and were recyclable for up to ten cycles.
  • COF encapsulation significantly enhanced BGL stability in 1-15% SDS solutions, mitigating denaturation.

Conclusions:

  • A robust one-pot aqueous synthesis strategy for enzyme-COF composites was established.
  • Enzyme-COF interactions are key to enhancing enzyme stability and reusability.
  • This approach offers a viable method for creating stable, reusable biocatalysts for demanding applications.