Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

8.7K
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...
8.7K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

4.1K
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...
4.1K
Enzymes02:34

Enzymes

82.6K
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...
82.6K
Enzyme Kinetics01:19

Enzyme Kinetics

98.7K
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...
98.7K
Introduction to Enzymes01:22

Introduction to Enzymes

19.4K
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...
19.4K
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

83.5K
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
83.5K

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Dual-Recognition AIEgens-Lysozyme Assemblies for Interpretable Machine Learning-Enabled Sensor Arrays: Toward Rapid and Transparent Surveillance of Microbial Threats.

Analytical chemistry·2026
Same author

Integrating catalytic hairpin assembly with the signal amplification revolution of nanosensing strategies for food safety assurance.

Food research international (Ottawa, Ont.)·2026
Same author

Convolutional Neural Network-Assisted Ultrasensitive Immunochromatographic Strips of <i>Salmonella typhimurium</i> through Bright Luminescence and Nano-Biointerfacial Affinity Leveraging Schiff-Base Chemistry-Confined Mechanism.

Journal of agricultural and food chemistry·2026
Same author

Rigid Restriction-Enabled Ultrabright Luminescence through Feather-like Metal-AIEgens Frameworks and Coupling the Collaborative Interfacial Recognition Mechanism for Pathogen Diagnosis.

Analytical chemistry·2026
Same author

Harnessing Phage-Based Nanosensors for Advancing Ultrasensitive Point-of-Care Detection of Foodborne Pathogenic Bacteria.

Journal of agricultural and food chemistry·2026
Same author

A molecular imprinting-switchable laccase-like nanozyme-based onsite self-calibrating assay of ethyl carbamate residues.

Food chemistry·2025

Video Experimental Relacionado

Updated: Sep 9, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

17.5K

Ingeniería sinérgica multidimensional para impulsar la catálisis de nanoenzimas

Yuechun Li1, Zhaowen Cui1, Chenxin Ji1

  • 1College of Food Science and Engineering, Northwest A&F University, 22 Xinong Road, Yangling, Shaanxi, 712100, China.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)
|August 29, 2025
PubMed
Resumen
Este resumen es generado por máquina.

Este estudio analiza estrategias de vanguardia para mejorar la catálisis de nanoenzimas mediante la integración de la morfología, la estructura electrónica, los estímulos externos y el aprendizaje automático. Estos avances tienen como objetivo desbloquear el potencial de las nanoenzimas para aplicaciones ambientales y de otro tipo.

Palabras clave:
estimulando la catálisis de las nanoenzimasestructura electrónicaregulación externaAprendizaje automáticoEstructura morfológica

Más Videos Relacionados

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

8.9K
Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

8.0K

Videos de Experimentos Relacionados

Last Updated: Sep 9, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

17.5K
Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

8.9K
Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

8.0K

Área de la Ciencia:

  • Ciencias de los materiales
  • Ingeniería de catálisis
  • Inteligencia artificial

Sus antecedentes:

  • Las nanoenzimas ofrecen un gran potencial para aplicaciones en la remediación ambiental y más allá.
  • La mejora de la actividad catalítica de las nanoenzimas sigue siendo un desafío importante.

Objetivo del estudio:

  • Analizar sistemáticamente las estrategias de vanguardia para impulsar la catálisis de nanoenzimas.
  • Desarrollar un marco teórico que integre la morfología, la estructura electrónica, la estimulación externa y el diseño asistido por aprendizaje automático (ML).

Principales métodos:

  • Análisis de las relaciones estructura-actividad basadas en nanoestructuras.
  • Discusión en profundidad de la optimización de la estructura electrónica (por ejemplo, centro de banda d, ingeniería de defectos).
  • Resumen de los mecanismos de regulación dinámica mediante estímulos externos (ultrasonido, luz, campo eléctrico).
  • Enfoque en el cribado de alto rendimiento impulsado por ML para el descubrimiento acelerado de nanoenzimas.

Principales resultados:

  • Elucidación de la relación entre la nanomorfología y el rendimiento catalítico.
  • Comprensión del papel de la estructura electrónica en la actividad catalítica.
  • Resumen del impacto de los estímulos externos en la regulación catalítica.
  • Destacando el papel de ML en el análisis de las complejas relaciones estructura-actividad.

Conclusiones:

  • La integración interdisciplinaria es clave para superar los cuellos de botella actuales en el desarrollo de nanoenzimas.
  • Este trabajo proporciona una nueva perspectiva para el avance de la nanozimología.
  • Desbloquear el potencial de las nanoenzimas para hacer frente a los desafíos globales.