Corn peptide (CP) was prepared from corn gluten meal by proteolysis with alkaline protease from alkalophilic Bacillus A-7. Free amino acids were not found in the CP product. Gel filtration on a Shodex OH-packed column revealed that the molecular weight distribution of the CP was less than about 2, 000, characteristic of dipeptides to decapeptides, i.e. oligopeptides. The amino acid pattern of CP was similar to that of corn gluten meal, which was rich in alanine and branched-chain amino acids, but poor in basic amino acids. The effect of the CP administration on alcohol metabolism was examined with SHR-SP, which were given ethanol orally through a gastric tube at the rate of 1.0g/kg. Prior administration of CP at 1.0g/kg resulted in fast disappearance of ethanol and its oxidative product acetaldehyde from the blood relative to the control without administration. Hence, it is suggested that CP, rather than its constituent amino acids such as alanine and proline, effectively takes part in enhancing the metabolism of ethanol as well as acetaldehyde.