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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.
 
Most enzymes...
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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.
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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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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Ribozymes02:47

Ribozymes

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...
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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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Enzyme Kinetics01:19

Enzyme Kinetics

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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.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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GENPLAT: an Automated Platform for Biomass Enzyme Discovery and Cocktail Optimization
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Eutectozymes as Soft Hybrid Materials for Advanced Biocatalysis.

Manuel Eduardo Martinez Cartagena1, Lucia Suarez1, Aitor Ontoria1

  • 1POLYMAT, Applied Chemistry Department, Faculty of Chemistry, University of the Basque Country UPV/EHU, Donostia-San Sebastián, Spain.

Advanced Materials (Deerfield Beach, Fla.)
|December 24, 2025
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Summary

Eutectozymes, enzyme-loaded gels from natural solvents, offer enhanced stability and catalytic function. These resilient biocatalysts show promise in environmental cleanup and fighting resistant bacteria.

Keywords:
biocatalysisdeep eutectic solventsenzyme immobilizationeutectogelseutectozymes

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Area of Science:

  • Biomaterials Science
  • Catalysis
  • Environmental Science

Background:

  • Developing soft hybrid materials with structural integrity, biocompatibility, and catalytic function is crucial for advanced biocatalysis.
  • Enzyme stability and activity under harsh conditions remain a significant challenge.

Purpose of the Study:

  • To introduce eutectozymes, a novel enzyme-loaded eutectogel system.
  • To enhance enzyme stability, substrate affinity, and catalytic efficiency using a unique architecture.

Main Methods:

  • Formulation of eutectogels using natural hydrophobic deep eutectic solvents (HES).
  • Stabilization of enzymes within a dual supramolecular polymeric network.
  • Evaluation of catalytic performance under various operational conditions (temperature, pH, organic solvents).

Main Results:

  • Eutectozymes demonstrated remarkable resilience and high catalytic efficiency and reusability.
  • The unique microcavity structure protected enzymes, enhancing stability and substrate affinity.
  • Achieved over 90% degradation of recalcitrant dyes and showed antimicrobial activity against resistant bacteria.

Conclusions:

  • Eutectozymes represent a transformative platform for heterogeneous biocatalysis.
  • The synergistic combination of HES and gel matrices offers a robust solution for enzyme stabilization.
  • Opens new possibilities in biotechnology, bioelectronics, and environmental technologies.