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Related Concept Videos

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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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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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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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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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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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.
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Measuring Enzymatic Stability by Isothermal Titration Calorimetry
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Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

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Practical insights on enzyme stabilization.

Carla Silva1, Madalena Martins1, Su Jing2

  • 1a Centre of Biological Engineering (CEB) , University of Minho , Braga , Portugal.

Critical Reviews in Biotechnology
|August 3, 2017
PubMed
Summary
This summary is machine-generated.

Enzymes offer efficient catalysis but struggle in extreme industrial conditions. This review practically explores enzyme stabilization strategies to enhance their industrial application and stability in harsh environments.

Keywords:
Stabilizationenzymesformulationindustrial catalysismolecular interactions

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Area of Science:

  • Biochemistry and Industrial Biotechnology

Background:

  • Enzymes are nature's catalysts, optimized for physiological conditions.
  • Industrial processes often require extreme conditions (e.g., high temperature, pH) that compromise enzyme stability.
  • Current strategies for enzyme isolation from extremophiles do not fully address industrial stability requirements.

Purpose of the Study:

  • To provide a practical overview of enzyme stabilization strategies.
  • To highlight case studies demonstrating the application of these strategies.
  • To bridge the gap between theoretical knowledge and practical implementation of enzyme stabilization.

Main Methods:

  • Literature review focusing on enzyme stabilization techniques.
  • Compilation of case studies illustrating practical applications.
  • Analysis of common and effective enzyme stabilization approaches.

Main Results:

  • Enzyme instability is a critical barrier to industrial implementation.
  • Various strategies exist for enhancing enzyme stability under extreme conditions.
  • Practical case studies demonstrate successful enzyme stabilization for industrial use.

Conclusions:

  • Effective enzyme stabilization is crucial for expanding biocatalysis in industry.
  • A practical approach to stabilization strategies can overcome limitations of current methods.
  • Further research and application of these techniques will enhance industrial enzyme utility.