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Related Concept Videos

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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Enzyme Inhibition01:30

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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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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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Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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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.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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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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Updated: Oct 23, 2025

Measuring Lactase Enzymatic Activity in the Teaching Lab
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Aiming for the Bullseye: Targeted activities decrease misconceptions related to enzyme function for undergraduate

Cassidy R Terrell1, Thomas Ekstrom1, Brian Nguyen1

  • 1Center for Learning Innovation, University of Minnesota, Rochester, Minnesota, USA.

Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology
|August 21, 2021
PubMed
Summary
This summary is machine-generated.

Active learning strategies and 3D models improved undergraduate biochemistry students' understanding of enzyme structure and function. While both methods boosted scores, 3D models did not show additional benefits in reducing misconceptions.

Keywords:
active learningassessment and the design of probes for student understanding and learningassessment of educational activitiesconcept inventoryenzyme substrate interactionsenzymes and catalysismolecular visualizationphysical models as learning tools

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Area of Science:

  • Biochemistry Education
  • Undergraduate Science Pedagogy

Background:

  • Abstract concepts in biochemistry, particularly enzyme structure and function, pose significant learning challenges for undergraduates.
  • Student misconceptions in biochemistry can impede overall conceptual understanding and academic progress.

Purpose of the Study:

  • To assess the effectiveness of targeted learning activities and 3D physical models in addressing undergraduate biochemistry student misconceptions.
  • To measure conceptual changes in enzyme-substrate interactions using the Enzyme-Substrate Interactions Concept Inventory (ESICI).

Main Methods:

  • An undergraduate biochemistry course implemented active learning activities, with one group using 3D physical models (Intervention) and a control group not.
  • The Enzyme-Substrate Interactions Concept Inventory (ESICI) was administered Pre- and Post-instruction to assess conceptual understanding and misconceptions.
  • Student performance was compared between the Intervention and Control groups, and against a national sample.

Main Results:

  • Both active learning strategies, with and without 3D models, significantly increased ESICI scores to a level comparable to the highest national performers.
  • Misconception markers decreased in both groups compared to the national sample, though specific misconceptions varied between groups.
  • No significant additional benefit was observed for the 3D physical model group in reducing misconception markers compared to active learning alone.

Conclusions:

  • Both active learning and the use of 3D physical models are effective pedagogical tools for enhancing conceptual understanding in undergraduate biochemistry.
  • While effective, several misconceptions persisted, suggesting a need for further refinement of teaching strategies and assessment tools.
  • The study recommends revising ESICI questions to improve assessment validity and suggests future research into optimizing pedagogical approaches.