Related Experiment Video

Updated: Mar 17, 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

16.9K

Yeast surface display of dehydrogenases in microbial fuel-cells

Idan Gal1, Orr Schlesinger1, Liron Amir1

  • 1Department of Life Sciences and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, P.O. Box 653, Beer-Sheva 84105, Israel.

Bioelectrochemistry (Amsterdam, Netherlands)
|July 27, 2016
PubMed

Keywords:
Cellobiose dehydrogenaseEnzymatic fuel cellsMicrobial fuel cellsPyranose dehydrogenaseYeast surface display

More Related Videos

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-109:00

Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1

Published on: April 16, 2018

10.8K
Waste Water Derived Electroactive Microbial Biofilms: Growth, Maintenance, and Basic Characterization11:58

Waste Water Derived Electroactive Microbial Biofilms: Growth, Maintenance, and Basic Characterization

Published on: December 29, 2013

14.2K

Related Concept Videos

Microbial Fermentation01:23

Microbial Fermentation

Fermentation is a crucial anaerobic metabolic process that enables microbes to derive energy from sugar without relying on oxygen or an electron transport chain. This process is fundamental to various biological and industrial applications and is classified based on the metabolic products generated.Role of Pyruvate in FermentationPyruvate and its derivatives serve as key electron acceptors in fermentative pathways. The oxidation of NADH to regenerate NAD+ is essential for the continuation of...
1.8K
Fates of Pyruvate01:20

Fates of Pyruvate

Pyruvate is the end product of glycolysis, where glucose is oxidized to pyruvate, simultaneously reducing NAD+ to NADH. Two molecules of ATP are also produced by substrate-level phosphorylation.
In aerobic organisms, pyruvate is metabolized via the citric acid cycle to produce reduced coenzymes NADH and FADH2. These coenzymes are then oxidized in the electron transport chain to produce ATP and, in the process, regenerate the NAD+ and FAD. As seen in some cell types and organisms, fermentation...
12.0K
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...
31.8K
Fermentation01:29

Fermentation

Most eukaryotic organisms require oxygen to survive and function adequately. Such organisms produce large amounts of energy during aerobic respiration by metabolizing glucose and oxygen into carbon dioxide and water. However, most eukaryotes can generate some energy in the absence of oxygen by anaerobic metabolism.
Fermentation is a type of metabolic process that occurs in the absence of oxygen, where organic molecules such as glucose are broken down to produce energy. During this process, the...
132.5K
Pyruvate Oxidation01:15

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
170.5K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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...
5.3K