Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

3.8K
Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
3.8K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

10.4K
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...
10.4K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

4.9K
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...
4.9K
Catalysis02:50

Catalysis

30.0K
The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
30.0K
Introduction to Enzymes01:22

Introduction to Enzymes

31.3K
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...
31.3K
Biosynthesis in Bacteria01:24

Biosynthesis in Bacteria

532
Biosynthesis in bacteria is a fundamental anabolic process that generates essential macromolecules, including proteins, nucleic acids, lipids, and polysaccharides. These macromolecules are critical for cellular growth, replication, and function. The process is tightly regulated and energetically linked to catabolic pathways to ensure optimal resource utilization.Biosynthetic pathways begin with precursor metabolites such as pyruvate, acetyl-CoA, and glucose-6-phosphate derived from glycolysis,...
532

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Multi-Level Asymmetric Mesoporous Nanochannels for Photothermal-Regulated Dopamine Sensing.

Angewandte Chemie (International ed. in English)·2026
Same author

Anatomical and Imaging Predictors of Peri-Device Leak Following Left Atrial Appendage Closure Using the LAmbre Device: A Comparative Study of CCTA and TEE.

Catheterization and cardiovascular interventions : official journal of the Society for Cardiac Angiography & Interventions·2026
Same author

AirDC: Adaptive Iterative Depth Refinement Framework for Full-Range Metric Depth Completion.

IEEE transactions on image processing : a publication of the IEEE Signal Processing Society·2026
Same author

Multi-omics and machine learning integration of diverse cell death pathways optimize risk stratification and inform drug therapy in Wilms tumor.

Discover oncology·2026
Same author

Effects of Simulated Service Environments on the Microstructure and Interfacial Properties of Ceramic Fiber-Reinforced Al-Matrix Composites.

Materials (Basel, Switzerland)·2026
Same author

Targeting Microbial Bile Salt Hydrolase Reprograms Bile Acid Metabolism and Ameliorates Metabolic Dysfunction-Associated Steatohepatitis in Mice.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jan 8, 2026

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

18.0K

Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.

Si Liu1,2, Peiji Deng1,2, Qianfan Chen1,2,3

  • 1School of Chemical Engineering, The University of New South Wales, Sydney, New South Wales, 2052, Australia.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|December 13, 2025
PubMed
Summary

Reticular materials like MOFs, COFs, and HOFs offer enzyme immobilization but often reduce performance. Strategies focus on material tuning, interface design, and protein engineering to enhance biocatalyst activity.

Keywords:
biocatalysiscovalent organic frameworksenzyme immobilizationhydrogen‐bonded organic frameworksmetal‐organic frameworks

More Related Videos

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
08:25

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs

Published on: January 17, 2020

7.7K
A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
07:59

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

Published on: October 4, 2019

10.3K

Related Experiment Videos

Last Updated: Jan 8, 2026

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

18.0K
Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
08:25

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs

Published on: January 17, 2020

7.7K
A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
07:59

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

Published on: October 4, 2019

10.3K

Area of Science:

  • Materials Science
  • Biochemistry
  • Nanotechnology

Background:

  • Reticular materials (MOFs, COFs, HOFs) are promising for enzyme immobilization due to their properties.
  • Enzyme performance is often reduced by encapsulation due to confinement and altered microenvironments.

Purpose of the Study:

  • To review strategies for enhancing enzyme activity within reticular materials.
  • To provide a multiscale perspective on improving enzyme encapsulation.

Main Methods:

  • Summarizing approaches from nano/macro material tuning, molecular interface design, and protein surface engineering.
  • Highlighting differences in enzyme activity enhancement across MOF-, COF-, and HOF-based composites.
  • Discussing nano-bio effects for customized biocatalytic functions.

Main Results:

  • Multiscale strategies can significantly boost enzyme performance in reticular materials.
  • Nano-bio effects enable the creation of nanobiohybrids with novel biocatalytic functions.
  • Differences exist in activity enhancement among MOF, COF, and HOF systems.

Conclusions:

  • Understanding molecular events is key to optimizing enzyme-framework interactions.
  • Advanced designs in heterogeneous biocatalysts are emerging from reticular chemistry.
  • Challenges and opportunities exist for translating these advancements into practical applications.