Related Experiment Video
Updated: Oct 31, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Chemo-bio catalysis using carbon supports: application in H2-driven cofactor recycling
Xu Zhao1, Sarah E Cleary1, Ceren Zor2
1Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory South Parks Road Oxford OX1 3QR UK holly.reeve@chem.ox.ac.uk kylie.vincent@chem.ox.ac.uk.
This study introduces novel chemo-bio catalysts for efficient, enantioselective hydrogenation using H2-driven NADH regeneration. These catalysts combine metal/carbon materials with enzymes for cleaner chemical synthesis.
Area of Science:
- Catalysis
- Biochemistry
- Green Chemistry
Background:
- Heterogeneous biocatalytic hydrogenation offers a sustainable route for enantioselective reductions.
- Enzyme-catalyzed reactions often require efficient cofactor regeneration systems, such as nicotinamide adenine dinucleotide (NADH).
- Hydrogen gas (H2) is a clean reductant, but its direct application in biocatalysis needs effective activation and cofactor recycling.
Purpose of the Study:
- To develop and characterize novel chemo-bio catalysts for direct H2-driven NAD+ reduction.
- To investigate the use of carbon-supported metal (metal/C) catalysts for H2 oxidation and electron transfer to adsorbed enzymes.
- To demonstrate the application of these integrated systems for enantioselective ketone reductions using alcohol dehydrogenase.
Main Methods:
- Commercial metal/C catalysts were evaluated for direct H2-driven NAD+ reduction.
- Selected metal/C catalysts were coupled with enzymes on conductive carbon supports for H2 oxidation and NAD+ reduction.
- Characterization of metal/C catalysts and carbon supports to identify key properties influencing activity.
- Optimized chemo-bio catalysts were used with alcohol dehydrogenase for enantioselective ketone reductions.
Main Results:
- Chemo-bio catalysts demonstrated improved activity and selectivity for generating bioactive NADH under ambient conditions.
- High cofactor turnover numbers and enzyme activities were achieved (e.g., 441 h-1 for Pd and 2347 h-1 for NAD+ reductase).
- Enantioselective ketone reductions proceeded with >99% enantiomeric excess (ee).
Conclusions:
- A novel strategy for combining chemo- and biocatalysis on carbon supports was successfully demonstrated.
- This integrated approach provides an efficient and sustainable method for producing bioactive NADH.
- The developed chemo-bio catalysts are effective for enantioselective hydrogenation reactions, offering a greener alternative to traditional methods.
More Related Videos
08:40Synthesis of Metal Nanoparticles Supported on Carbon Nanotube with Doped Co and N Atoms and its Catalytic Applications in Hydrogen Production
Published on: December 6, 2021
10:57Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction
Published on: April 10, 2018
Related Concept Videos
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation
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...
Catalysis
Reduction of Alkenes: Catalytic Hydrogenation
Metals like palladium, platinum, and nickel are commonly used in their solid forms — fine powder on an inert surface. As these catalysts remain insoluble in the reaction mixture, they are referred to as heterogeneous catalysts.
The hydrogenation process takes place on the...
Reduction of Benzene to Cyclohexane: Catalytic Hydrogenation
Reduction of Alkynes to cis-Alkenes: Catalytic Hydrogenation
Like alkenes, alkynes can be reduced to alkanes in the presence of transition metal catalysts such as Pt, Pd, or Ni. The reaction involves two sequential syn additions of hydrogen via a cis-alkene intermediate.
Introduction to Mechanisms of Enzyme Catalysis