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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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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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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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Human civilization relies on biodiversity in many ways. Sudden changes in species biodiversity result in environmental changes that can modify weather patterns and therefore human civilizations.
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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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Engineering Enzymes for Environmental Sustainability.

Emily Radley1, John Davidson1, Jake Foster1

  • 1Department of Chemistry & Manchester Institute of Biotechnology The University of Manchester 131 Princess Street Manchester M1 7DN UK.

Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)
|March 22, 2024
PubMed
Summary
This summary is machine-generated.

Engineered enzymes offer sustainable solutions for net-zero targets by capturing carbon dioxide, degrading pollutants, recycling plastics like polyethylene terephthalate (PET), and converting biomass into biofuels, advancing a cleaner chemical industry.

Keywords:
BiocatalysisDirected EvolutionEnzyme EngineeringSustainability

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Sustainable Chemistry
  • Environmental Biotechnology

Background:

  • Achieving net-zero targets necessitates sustainable catalytic technologies.
  • Engineered enzymes, particularly through directed evolution, are crucial for environmental conservation and process sustainability.
  • Biocatalysis offers a pathway to greener chemical processes.

Purpose of the Study:

  • To review the deployment of engineered enzymes in sustainable industrial processes.
  • To highlight the role of directed evolution in creating robust biocatalysts.
  • To illustrate the contribution of enzyme engineering to a cleaner chemical industry.

Main Methods:

  • Review of literature on engineered enzymes and biocatalysis.
  • Focus on directed evolution techniques for enzyme refinement.
  • Analysis of applications in CO2 capture, bioremediation, plastic recycling, and biomass conversion.

Main Results:

  • Engineered enzymes efficiently capture carbon dioxide (CO2) and are integrated into metabolic pathways.
  • Enzymes have been refined for enhanced bioremediation of toxic pollutants.
  • Biocatalytic depolymerization of polyethylene terephthalate (PET) using engineered cutinases and PETases is advancing plastic recycling.
  • Optimized enzymes facilitate the conversion of plant biomass into biofuels and valuable chemicals.

Conclusions:

  • Enzyme engineering and biocatalysis are vital for developing sustainable chemical industries.
  • Directed evolution enables the creation of enzymes for diverse environmental and industrial applications.
  • Biocatalytic approaches contribute significantly to achieving net-zero emissions and environmental protection.