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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...
Introduction to Enzymes01:22

Introduction to Enzymes

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 bind the substrates and convert them into products. Many enzymes also...
Introduction To Enzymes01:22

Introduction To Enzymes

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 bind the substrates and convert them into products. Many enzymes also...
Enzymes02:34

Enzymes

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...
Enzyme Kinetics01:19

Enzyme Kinetics

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...
Microbial Biosensors01:17

Microbial Biosensors

Microbial biosensors are analytical devices that utilize living microbes to detect specific substances through measurable signals. These devices consist of two main components: biosensing organisms and signal-transducing elements. Biosensing organisms, such as Escherichia coli or Saccharomyces cerevisiae, are typically housed in multiwell plates connected to transducers, enabling rapid, real-time detection of target analytes.Signal Generation MechanismWhen a target analyte—such as...

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Updated: Jun 21, 2026

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
06:51

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits

Published on: September 20, 2016

Enzymatic substrates in microbiology.

Sylvain Orenga1, Arthur L James, Mohammed Manafi

  • 1Research & Development Microbiology, bioMérieux, 3 route de Port Michaud, La Balme-les-Grottes, France. sylvain.orenga@eu.biomerieux.com

Journal of Microbiological Methods
|August 15, 2009
PubMed
Summary
This summary is machine-generated.

Synthetic enzymatic substrates enhance microbial detection and identification in various assays. These advanced tools improve accuracy and speed compared to traditional methods, remaining valuable in modern diagnostics.

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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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Area of Science:

  • Biochemistry
  • Microbiology
  • Synthetic Chemistry

Background:

  • Enzymatic substrates are crucial tools in biochemistry and microbiology.
  • They are used for studying metabolic pathways and identifying microorganisms.
  • Synthetic substrates offer customized properties for advanced microbial assays.

Purpose of the Study:

  • To review the advancements and applications of synthetic enzymatic substrates in microbiology.
  • To highlight their role in improving the detection, enumeration, and identification of microorganisms.
  • To emphasize their continued relevance alongside molecular biology techniques.

Main Methods:

  • Review of literature on synthetic enzymatic substrates in microbiology.
  • Analysis of their application in multi-test systems and chromogenic media.
  • Comparison with conventional methods using natural substrates.

Main Results:

  • Synthetic enzymatic substrates have expanded significantly over the past 20 years.
  • New substrates offer improved spectral, chemical, and biochemical properties.
  • These substrates enhance the detection of food-borne pathogens, clinical isolates, and resistant bacteria.
  • They enable faster and more specific microbial identification compared to natural substrates.

Conclusions:

  • Synthetic enzymatic substrates are indispensable tools in modern microbiology.
  • They facilitate improved diagnostics for a wide range of microorganisms in diverse sample types.
  • Phenotypic tests using these substrates remain valuable for analyzing complex samples in diagnostic and research settings.