Alcohol Dehydrogenase

Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.
Off-white lyophilized powder, soluble in water, pI 5.4, optimum pH 8.6-9.0 (ethanol oxidation) or 7.0 (aldehyde reduction). Stability: high concentration of nearly neutral enzyme in pure water can be stable for several days at 5℃, unstable in acidic (pH lower than 6.0) and alkaline (pH greater than 8.5) solution; adding glutathione, cysteine or serum albumin to dilute solution can increase its stability; lyophilized powder containing sucrose and phosphate, stored at 4℃ for six months, the vitality is reduced by 10%; crystal suspension containing phosphate, stored at 4℃ for six months, the vitality is reduced by 40%. Crystallized suspension containing phosphate, 40% reduction in viability for six months at 4°C. Activators include mercaptoethanol, dimercaptosuccinol, cysteine and heavy metal chelators; inhibitors include heavy metals and sulfhydryl reagents. Enzymatic reaction: alcohol + coenzyme I ═ aldehyde or ketone + reduced coenzyme I.
This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research.