Multi-enzyme catalyzed rapid ethanol lowering in vitro.
Ethanol was oxidized to acetate by an enzyme system using yeast alcohol dehydrogenase (YADH), yeast aldehyde dehydrogenase (YALDH), and lactic dehydrogenase (LDH) recycling NAD in two model duodenal fluids and in canine duodenal aspirate in vitro. Sufficient enzyme activities were maintained to convert as much as 34% of the original ethanol to acetate with negligible acetaldehyde accumulation.
Whitmire
D R
DR
Department of Biological and Agricultural Engineering, University of Georgia, Athens 30602.
Chambers
R P
RP
Dillon
A R
AR
D000079:Acetaldehyde / Q000378:metabolism; D000085:Acetates / Q000378:metabolism; D000426:Alcohol Dehydrogenase / Q000502:physiology*; D000444:Aldehyde Dehydrogenase / Q000502:physiology*; D000818:Animals; D004285:Dogs; D004386:Duodenum / Q000201:enzymology*; D000431:Ethanol / Q000493:pharmacokinetics*; D005766:Gastrointestinal Contents / Q000201:enzymology; D007770:L-Lactate Dehydrogenase / Q000502:physiology*; D009243:NAD / Q000378:metabolism; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid
D000085:Acetates; D011773:Pyruvates; D009243:NAD; D000431:Ethanol; D019289:Pyruvic Acid; D000426:Alcohol Dehydrogenase; D007770:L-Lactate Dehydrogenase; D000444:Aldehyde Dehydrogenase; D000079:Acetaldehyde