Effect of arginine on the alcohol dehydrogenase and acetaldehyde dehydrogenase enzymes of alcohol metabolism in Saccharomyces cerevisiae.

Abstract

Arginine possesses advantageous pharmacological properties such as liver injury protection. We have previously shown that the arginine stimulated the activities of commercial alcohol dehydrogenase (ADH, EC 1.1.1.1) and acetaldehyde dehydrogenase (ALDH, EC 1.2.1.10) enzymes in vitro experiment. We therefore examined on the activities, zymogram staining intensity, and protein expression of alcohol metabolizing ADH and ALDH in Saccharomyces cerevisiae cultured in a medium supplemented with different concentrations of arginine. The enhanced activity, zymogram staining intensity, and protein expression of ADH in the cell-free extracts of S. cerevisiae showed at 0.01 and 0.05% (w/v) arginine supplementation. These parameters of ALDH in the cell-free extracts of S. cerevisiae showed in the 0.005-0.05% arginine treatment concentration, but these parameters were shown to be decreased at a concentration of 0.1% (w/v) arginine, which was the highest supplementation. These results indicate that arginine can be used to enhance the enzyme activities, staining intensity for the protein activity in the zymogram analysis, and increased protein expression of ADH and ALDH in S. cerevisiae. These results also indicate that arginine can be used to the protection of alcoholic liver injury and hangover by strong activation of alcohol metabolizing ADH and ALDH.