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

Biofuels01:25

Biofuels

The microbial conversion of organic matter into biofuels holds potential as a renewable energy source. Among biofuel sources, microalgae are recognized as a highly efficient and adaptable feedstock for biodiesel production, owing to their rapid biomass accumulation, elevated lipid productivity, and capacity to proliferate in diverse aquatic systems, including freshwater, marine, and wastewater habitats. Unlike terrestrial crops, microalgae do not compete for land and can achieve significantly...
Batteries and Fuel Cells03:12

Batteries and Fuel Cells

A battery is a galvanic cell that is used as a source of electrical power for specific applications. Modern batteries exist in a multitude of forms to accommodate various applications, from tiny button batteries such as those that power wristwatches to the very large batteries used to supply backup energy to municipal power grids. Some batteries are designed for single-use applications and cannot be recharged (primary cells), while others are based on conveniently reversible cell reactions that...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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.
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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.
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...

You might also read

Related Articles

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

Sort by
Same author

Reduced mediators released by cyanobacteria during exoelectrogenesis detected using differential pulse voltammetry.

Bioelectrochemistry (Amsterdam, Netherlands)·2026
Same author

An Automated Electrochemistry Platform for Accelerating the Characterization of Enzymatic Electrochemistry.

ACS electrochemistry·2026
Same author

Closing the nitrogen loop in groundwater with biohybrid technologies.

Trends in biotechnology·2026
Same author

Mass Spectrometry Imaging in ACS Journals.

ACS measurement science au·2026
Same author

High-throughput Optical Analysis to Inform Design of Electrochemical Biosensors.

ACS measurement science au·2026
Same author

Data-Driven Electrochemistry Reveals the Impact of Hydrophobicity on Aptamer Cross-Reactivity.

ACS measurement science au·2026

Related Experiment Video

Updated: May 26, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Enzymatic biofuel cells utilizing a biomimetic cofactor.

Elliot Campbell1, Matthew Meredith, Shelley D Minteer

  • 1Department of Chemical Engineering, Columbia University in the City of New York, New York, NY 10027, USA.

Chemical Communications (Cambridge, England)
|January 10, 2012
PubMed
Summary

Engineered enzymes using nicotinamide mononucleotide (NMN(+)) improve immobilized systems by overcoming cofactor limitations. This approach enhances performance despite a slower turnover rate with the minimal cofactor.

More Related Videos

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

Solar-Driven Electrochemical Green Fuel Production from CO2 and Water Using Ti3C2Tx MXene-Supported CuZn and NiCo Catalysts
10:15

Solar-Driven Electrochemical Green Fuel Production from CO2 and Water Using Ti3C2Tx MXene-Supported CuZn and NiCo Catalysts

Published on: November 7, 2025

Related Experiment Videos

Last Updated: May 26, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

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

Solar-Driven Electrochemical Green Fuel Production from CO2 and Water Using Ti3C2Tx MXene-Supported CuZn and NiCo Catalysts
10:15

Solar-Driven Electrochemical Green Fuel Production from CO2 and Water Using Ti3C2Tx MXene-Supported CuZn and NiCo Catalysts

Published on: November 7, 2025

Area of Science:

  • Biocatalysis and enzyme engineering
  • Biotechnology
  • Biochemical engineering

Background:

  • Immobilized enzyme systems are crucial for industrial biocatalysis.
  • Cofactor diffusion and regeneration are key limitations in enzyme performance.
  • Nicotinamide adenine dinucleotide (NAD)-dependent enzymes are widely used but require efficient cofactor recycling.

Purpose of the Study:

  • To engineer an enzyme system that overcomes cofactor limitations in immobilized biocatalysis.
  • To evaluate the performance of an engineered enzyme utilizing nicotinamide mononucleotide (NMN(+)) as a minimal cofactor.
  • To assess the impact of NMN(+) on cofactor diffusion and regeneration in immobilized enzyme systems.

Main Methods:

  • Enzyme engineering to create a variant capable of utilizing NMN(+).
  • Immobilization of the engineered enzyme system.
  • Performance evaluation of the immobilized system with NMN(+) compared to traditional cofactors.
  • Analysis of cofactor diffusion and regeneration rates.

Main Results:

  • The engineered enzyme successfully utilized NMN(+) as a cofactor.
  • Significant performance gains were observed in immobilized systems employing NMN(+).
  • A decreased turnover rate was noted with NMN(+) despite overall performance improvements.

Conclusions:

  • Utilizing NMN(+) with engineered enzymes offers a viable strategy to enhance immobilized enzyme system performance.
  • This approach effectively addresses cofactor diffusion and regeneration challenges.
  • Further research can optimize turnover rates for broader applications.