• Journal of Life Science
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• v.19 no.9
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• pp.1321-1327
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• 2009

The present study examined the comparative effects of various amino acids on the alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities of yeast Saccharomyces cereviciae and rat liver homogenate in vitro. Methionine showed the highest activity in yeast ADH among the amino acids used in this study, but this was not higher than that of the hangover product, Condition-Power (CP) used as positive control. Methionine was also found to be the best amino acid in terms of the ALDH activity in rat liver homogenate among the treatment amino acids, which was comparatively higher than that of positive control CP. It was chosen for further experiments and yeast ADH activity increased in parallel with increased methionine concentration, but not rat liver ALDH activity, and it was comparatively higher than those of the positive control. Arginine showed the highest values in yeast ALDH and rat liver ADH activities among amino acids, and it was chosen for further experiments. Yeast ALDH activity increased in parallel with increased arginine concentration, which was higher than that of positive control CP, and rat liver ADH activity was also comparatively higher in all treatment concentrations of arginine than that of positive control CP. The native electrophoresis of ADH and ALDH from cell-free extracts of yeast Saccharomyces cerevisiae cultured in the growth medium containing various arginine concentrations by $0{\sim}0.1%$ showed two active bands upon zymogram staining analysis, and the straining intensity of ADH and ALDH active bands in arginine treatment yeast was stronger than that of non-yeast or low treatment yeast. These results indicate that alcohol metabolizing enzyme activities can be enhanced by arginine and methionine, suggesting that arginine and methionine have potent ethanol-metabolizing activities.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.1
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• pp.27-32
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• 1985

For the purpose of investigating the influence of pollen load un alcohol metabolism in rat, we analyzed quantitatively amino acids of pollen load, and investigated the changes of hepatic alcohol dehydrogenase(ADH) activity and hepatocyte morphology in rat administrated various concentrations of alcohol and various amounts of pollen load. 18 species of amino acids including phenylalanine in the sunflower pollen load were quantitatively analyzed, and it was found that the amount of phenylalanine, leucine, threonine, lysine are especially higher than that of the other amino acids. The liver ADH activity of experimental animals decreased with the proportion of ethanol concentration much more in ethanol administrated group than in control group, while increased in pollen load mixed with ethanol administrated group, but didn't increased as much as that in control group. In any case the less the degree of ethanol concentration was administrated, the higher the liver ADH activity increased. There was fat infiltration in the hepatocyte of ethanol administrated animals, and remarkably little fat infiltration in that of animals administrated pollen load mixed with ethanol.

• Korean Journal of Food Science and Technology
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• v.36 no.2
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• pp.329-332
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• 2004

Changes in activities of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) in vitro were examined by measuring maximum absorbances of ADH and ALDH at 340 nm to determine influence of Maesil (Prunus mume) on alcohol metabolism. Facilitating rates of ADH activity were 137.92, 131.58, 152,96, 218.70, 111.76, and 144.27% in Maesil juice, 5, 10, and 15% GMT, and 0.5 and 1.0% aspartic acid, respectively, ALDH activity increased in the order of Maesil juice > ALDH > GMT > aspartic acid, and facilitating rate of ALDH activity in Maesil juice was the highest at 976.44%. These results indicate alcohol metabolizing activity can be enhanced by Maesil juice.

• Applied Biological Chemistry
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• v.39 no.1
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• pp.1-8
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• 1996

A one-stage, continuous-flow bioreactor with both immobilized and suspended cells was used to investigate the roles of lipid supplements in ethanol production by Saccharomyces cerevisiae. The reactor performance and the level of alcohol dehydrogenase(ADH) activities of the suspended cells, grown under various conditions, were measured. When ergosterol and/or oleic acid were added with surfactants to the yeast culture grown under non-aerated conditions, remarkable increases in ethanol production and cell growth was achieved, but specific ADH activities were not affected. Especially, no difference of specific ADH activities of the suspended cells grown under aerated and non-aerated condition was observed. The addition of the surfactant as a supplement also resulted in significant increases in ethanol production, cell growth, and specific ADH activity. When ergosterol and oleic acid were added to the yeast culture exposed to higher ethanol concentration($>40\;g/{\ell}$) level, ethanol production, cell growth, and specific ADH activity were increased, but the addition of surfactant was as effective as at lower ethanol concentration level. The results indicated that lipid supplements were more effective at higher ethanol concentration level than at lower ethanol concentration level during ethanol production. ADH isozyme patterns of the yeast cultures grown under various conditions on starch gel electrophoresis showed only one major band, probably ADH I. The migrating distance of the major isozyme, however, varied slightly according to the culture conditions of the cells. No apparent correlation was found between specific ADH activity and amount of ethanol produced. Cell mass was more important factor for ethanol production than specific ADH activity of the cells.

• Applied Biological Chemistry
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• v.42 no.2
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• pp.162-165
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• 1999

Effects of compounds isolated from Ainsliaea acerifolia on alcohol metabolism in rats were examined and the results were as follows: Apigenin $7-O-{\beta}-D-glucoside$, after a single oral administration to rats, was found to cause a significant decrease in the serum ethanol concentration as well as enhancement of liver cytosolic alcohol dehydrogenase(ADH) activity.

• Journal of Plant Biotechnology
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• v.47 no.2
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• pp.172-178
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• 2020

Fruit-specific promoters play an important role in the improvement of traits, such as fruit quality through genetic engineering. In tomato, the development of fruit-specific promoters was previously reported, but less attention has been paid to the promoters involved in the fruit development stage. In this study, we characterized the gene expression patterns of tomato alcohol dehydrogenase 2 (SlAdh2) in various tissues of wild-type tomato (cv. Ailsa Craig). Our findings revealed that SlAdh2 expression levels were higher in the developing fruit than in the leaves, stems, and flowers. The ProSlAdh2 region, which is expressed at different stages of fruit development, was isolated from tomato genomic DNA. Following this, it was fused with a β-glucuronidase reporter gene (GUS) and introduced into wild-type tomato using Agrobacterium-mediated transformation to evaluate promoter activity in the various tissues of transgenic tomato. The ProSlAdh2:GUS promoter exhibited strong activity in the fruit and weak activity in the stems, but displayed undetectable activity in the leaves and flowers. Interestingly, the promoter was active from the appearance of the green fruit (1 cm in size) to the well-ripened stage in transgenic tomatoes, indicating its suitability for transgene expression during fruit development and ripening. Thus, our findings suggest that ProSlAdh2 may serve as a potential fruit-specific promoter for genetic-based improvement of tomato fruit quality.

• Journal of Applied Biological Chemistry
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• v.65 no.3
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• pp.183-187
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• 2022

The hot water extract from cinnamon (Cinnamomum cassia Presl) inhibited the activity of alcohol dehydrogenase (ADH) with IC₅₀ value of 45.6 ㎍/mL. The ADH inhibitory components in cinnamon extract were relatively stable to acid and heat, but were found to be volatile. The optimum temperature and time for extracting the ADH inhibitory components from cinnamon were 80 ℃ and 2 h, respectively. Among the essential oils of cinnamon, cinnamaldehyde was the main substance for ADH inhibition. Cinnamaldehyde is considered a competitive inhibitor of ethanol to ADH. Therefore, the cinnamon extract and cinnamaldehyde showed the potential to be used as natural materials for relieving symptoms of a hangover.

• Microbiology and Biotechnology Letters
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• v.25 no.4
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• pp.386-390
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• 1997

The characteristics of alcohol dehydrogenase (ADH, EC 1.1.1.1, alcohol:NAD oxidoreductase) of thermotolerant alcohol-producing yeasts, Saccharomyces cerevisiae RA-74-2 and Kluyveromyces marxianus RA-912, were compared with that of mesophilic S. cerevisiae D, an industrial strain. Under anaerobic culture condition, both S. cerevisiae RA-74-2 and D had similar level of ADH activity at 30$\circ$C, and the activity of S. cerevisiae RA-74-2 at 37$\circ$C was the same level at 30$\circ$C. However, the level of ADH activity of S. cerevisiae D at 37$\circ$C decreased about 70% of that at 30$\circ$C. The level of enzyme activity of K. marxianus RA-912, which showed lower alcohol productivity than S. cerevisiae RA-74-2 and D, was about 43% of those strains at 30$\circ$C, and decreased somewhat at 37$\circ$C. The results showed a good correlation between the alcohol productivities and the level of ADH activities of these strains grown at 30$\circ$C and 37$\circ$C. And the higher heat stability of ADH of S. cerevisiae RA-74-2 than that of S. cerevisiae D seemed to reflect the ability of high temperature fermentation. Despite of its fermentation ability even at 45$\circ$C, however, the ADH of K. marxianus RA-912 showed lower heat stability than that of S. cerevisiae D. Both S. cerevisiae RA-74-2 and D showed similar patterns of two bands of ADH isozyme, and the low band of S. cerevisiae RA-74-2 moved slightly faster than that of S. cerevisiae D. The staining intensity of the bands of S. cerevisiae D at 37$\circ$C was weaker than those at 30$\circ$C. However, S. cerevisiae RA-74-2 showed no differences in total intensity of the bands of 30$\circ$C and 37$\circ$C. As the patterns of cellular proteins and ADH isozyme of K. marxianus RA-912 were different from S. cerevisiae RA-74-2 and D, K. marxianus might have its own characteristic ADH system.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.521.3-522
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• 1986

A gene encoding alcohol dehydrogenase (ADH) in Zymomonas mobilis was cloned into E. coli JM 83 with plasmid pUC 9. The ADH produced by the E. coli transformant was purified bysonication, (NH$^4$)2SO4 fractionation, Affi-Gel blue and hydroxylapatite chromatography. The ADH produced by Z. mobilis was also purified by the same procedures. The two enzyme preparations were characterized and compared. It was found that the E. coli ADH was identical to one of two ADH isozymes of Z. mobilis. Analytical gel filtrations led to the conclusion that the molecule of E. coli ADH was composedv of four subunits having molecular weight of 40,000 (+1,000) dalton each The effect of metal ions on ADH activity and optimum pH were investigated.

• Korean Journal of Pharmacognosy
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• v.26 no.2
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• pp.148-153
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• 1995

As an initial step for evaluating hepatoprotective components against alcohol-induced toxicity, the effect of various fractions from Aloe vera on alcohol metabolism in rats were examined and the results were as follows: Water soluble fraction, after a single oral administration to rats, was found to cause a significant decrease in the serum ethanol concentration as well as enhancement of liver cytosolic ADH activity. On the other hand, the fractions soluble in organic solvent was found to cause an increase in the blood ethanol concentration and inhibit ADH activity. Further fractionation of the water soluble fraction by ultrafiltration system gave four subfractions corresponding to molecular weight and treatment of them in rats demonstrated that subfraction of M.W. > 30,000 exhibited the most potent enhancing activity of ethanol methabolism.