• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.679-683
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• 2001

This study was purposed to compare the activity of alcohol dehydrogenase and antioxidative effects of several plant extracts in the alcohol-treated rat liver. Sprague-Dawley rat weighing about 200 g were divided into the following 6 groups : normal, alcohol group and 4 different plant extracts administrated groups(Soybean sprout, Pine needle, Lentinus edodes, acanthopanacis cortex). Each plant extract was administrated orally by 200mg/kg b.w./day for 8 days before the alcohol treatment (5 g of 30% alcohol /kg b.w. by i.p.injection). All rats were sacrificed at 90 min after the alcohol treatment. The alcohol concentrations in serum of Soybean sprout and pine needle group were significantly lower than the Lentinus edodes and Acanthopanacis cortex group. The activity of alcohol dehydrogenase in the hepatic cytosol of Soybean sprout and Pine needle group was also significantly higher than the alcohol and the other groups However, the activity of catalase seemed not to be affected, although the extract groups showed slightly higher activities of catalase than the alcohol group. These results may indicate that the extracts of Soybean sprout and Pine needle were relatvely effective on the alcohol degradation. the activity of blutathione-peroxidase and lipid peroxidaton of all of the extract groups were significantly lower than the activity of alcohol group. These results can suggest that all of the use plant extracts more or less have an antioxidative effect on the alcohol-induced oxidation and especially, extracts of Soybean sprout and Pine needle have an stimulating effect on the alcohol absorption and degradation.

• Journal of Microbiology and Biotechnology
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• v.21 no.8
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• pp.791-795
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• 2011

Sea tangle, a kind of brown seaweed, was fermented with Lactobacillus brevis BJ-20. The gamma-aminobutyric acid (GABA) content in fermented sea tangle (FST) was 5.56% (w/w) and GABA in total free amino acid of FST was 49.5%. The effect of FST on the enzyme activities and mRNA protein expression of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) involved in alcohol metabolism in Saccharomyces cerevisiae was investigated. Yeast was cultured in YPD medium supplemented with different concentrations of FST powder [0, 0.4, 0.8, and 1.0% (w/v)] for 18 h. FST had no cytotoxic effect on the yeast growth. The highest activities and protein expressions of ADH and ALDH from the cell-free extracts of S. cerevisiae were evident with the 0.4% and 0.8% (w/v) FST-supplemented concentrations, respectively. The highest concentrations of GABA as well as minerals (Zn, Ca, and Mg) were found in the cell-free extracts of S. cerevisiae cultured in medium supplemented with 0.4% (w/v) FST. The levels of GABA, Zn, Ca, and Mg in S. cerevisiae were strongly correlated with the enzyme activities of ADH and ALDH in yeast. These results indicate that FST can enhance the enzyme activities and protein expression of ADH and ALDH in S. cerevisiae.

• Food Science and Preservation
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• v.15 no.1
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• pp.155-160
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• 2008

This study was conducted to examine the volatile flavor compounds of Hahyangju, a traditional Korean liquor, and to evaluate the effect of the beverage on alcohol metabolism in rats. By GC/MS analysis, 17 volatile flavor compounds including iso-butyl alcohol and iso-amyl alcohol were detected in Hahyangju. The concentrations of acetaldehyde and ethylacetate in Hahyangju were decreased by filtration. Alcohol (0.035 mg/dL) and acetaldehyde (0.29 mg/dL) levels in the blood of rats given Hahyangju (HT animals) were lower than in rats given 17% (v/v) alcohol (AT rats). Also, alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities in HT rats were $24.63{\pm}1.8{\mu}$moles/mg protein and $9.8{\pm}1.3{\mu}$moles/mg protein, respectively, and were higher than in AT animals. The increases in ADH and ALDH activity in HT animals resulted in decreases in alcohol and acetaldehyde concentrations in blood, compared to the levels seen in rats given 17% (v/v) alcohol. These results suggest that Hahyangju may increase alcohol metabolizing activity, and consumption of Hahyangju may result in less of a hangover than follows ingestion of beverages (such as wine) containing about 17% (v/v) alcohol.

• Journal of Food Hygiene and Safety
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• v.30 no.1
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• pp.115-119
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• 2015

${\beta}$-cyclodextrin has an ability to protect compounds from oxidative reaction by collecting them within its ring-like structure. So, In harsh condition ($40^{\circ}C$), marker compound, quercetin, was dramatically reduced in Hovenia dulcis fruit extract containing dextrin at 4 and 8 week compared to 0 week, but not that containing ${\beta}$-cyclodextrin. To evaluate the effects of dextrin and ${\beta}$-cyclodextrin on protective effect of H.dulcis fruit extract against alcohol-induced liver damage, The mice were orally injected alcohol, H. dulcis fruit extract/dextrin (HD) and H. dulcis fruit extract/${\beta}$-cyclodextrin (HCD), respectively, for 7 days. The mice orally administrated with alcohol significantly enhanced the serum concentration of alanine aminotransferase (ALT) and aspartate aminotransferase (AST) and the activity of lactate dehydrogenase (LDH) in serum compared to the control group. HD and HCD significantly decreased the levels of serum ALT and AST and serum LDH activities compared to alcohol group. And also alcohol group significantly increased the level of total cholesterol compared to the control group, but HD and HCD significantly reduced it compared to the alcohol group. However, the levels of TG in blood were not significantly changed in all groups. The activities of alcohol dehydrogenase (ADH) were significantly increased in HD and HCD group although those of aldehyde dehydrogenase showed an increasing tendency. This data suggested that HD and HCD were able to induce alcohol degradation in the liver tissues. All together, the results showed that HCD demonstrated their ability to protect liver from alcohol-induced damage on equal terms with HD.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.43 no.1
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• pp.1-5
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• 2010

Alcohol metabolizing activity of fermented sea tangle juice (FSYJ) using Lactobacillilus brevis BJ20 were evaluated by measuring relative alcohol dehydrogenease (ADH) and aldehyde dehydrogenase (ALDH) activities. According to the results of MTI assay. the fermented sea tangle juice by Lactobacillilus brevis BJ20 appeared safe in the cytotocxity. The relative ADH activity of FSTJ showed 124% at 10 mg/mL, which increased with increasing concentration. The relative ALDH activity showed, however, insignificant difference (P>0.05) between concentrations of FSTJ up to 50 mg/mL. These results suggested that fermented sea tangle juice by L. brevis BJ20 could be used as a potential material for metabolizing alcohol.

• Advances in Traditional Medicine
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• v.7 no.3
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• pp.311-320
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• 2007

The present study was designed to estimate the protective effect of (-) epigallocatechin gallate (EGCG) on ethanol-induced liver injury in rats. Chronic ethanol administration (6 g/kg/day ${\times}$ 60 days) caused liver damage that was manifested by the elevation of markers of liver dysfunction - aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, lactate dehydrogenase, bilirubin and ${\gamma}$-glutamyl transferase in plasma and reduction in liver glycogen. The activities of alcohol metabolizing enzymes such as alcohol dehydrogenase and aldehyde dehydrogenase were found to be altered in alcohol-treated group. Ethanol administration resulted in the induction of cytochrome p450 and cytochrome-$b_{5}$ activities and reduction of cytochrome-c reductase and glutathione-S-transferase, a phase II drug metabolizing enzyme. Further, ethanol reduced the viability of isolated hepatocytes (ex vivo) as assessed by trypan blue exclusion test and induced hepatocyte apoptosis as assessed by propidium iodide staining. Treatment of alcoholic rats with EGCG restored the levels of markers of liver injury and mitigated the alterations in alcohol metabolizing and drug metabolizing enzymes and cyt-c-reductase. Increased hepatocyte viability and reduced apoptotic nuclei were observed in alcohol + EGCG-treated rats. These findings suggest that EGCG acts as a hepatoprotective agent against alcoholic liver injury.

• Journal of Environmental Health Sciences
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• v.49 no.2
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• pp.99-107
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• 2023

Background: Excessive alcohol consumption is at the root of serious social problems such as hangovers, liver dysfunction, and alcoholism. Objectives: This study was carried out to determine the hangover ameliorating effect of fermented rice extract and a combination of yeast-fermented powder and lysate containing aldehyde dehydrogenase (ALDH) (improved new ingredients) in an ethanol-induced rat study. Methods: The concentrations of alcohol, acetaldehyde, and malondialdehye in serum were evaluated to assess the anti-alcohol and anti-aldehyde hangover effect in two experiments, one with fermented rice extract) and a second with yeast-fermented powder and lysate, using animal studies. Results: Experiment 2 with yeast-fermented powder and lysate containing ALDH showed similar and higher activity, respectively, in reducing ethanol and acetaldehyde concentration compared with Experiment 1 with fermented rice extract. Experiment 2 also significantly reduced malondialdehyde, a type of lipid peroxide. The ALDH-related compound (ARC) lysate showed better hangover relief effect than ARC powder. Conclusions: These results indicate that ALDH-related compounds exhibit a hangover relief effect, and fermented lysate is considered to be a better candidate for hangover relief.

• International Journal of Industrial Entomology and Biomaterials
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• v.7 no.1
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• pp.51-57
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• 2003

A cDNA encoding a putative alcohol dehydrogenase (ADH) class III was cloned from the silkworm, Bombyx mono The full length cDNA is 1,385 nucleotides long and contains an open reading frame of 1,128 bp encoding 376 amino acid residues. The B. mon ADH III protein sequence was aligned with ADH III known from various organisms. Interestingly, the protein sequence of B. mon ADH III showed 87% and 85% identity to ADH III from marine fish Sparus aurata and Branchiostoma floridae, respectively, whereas rather low sequence identity (83%) to Drosophila melanogaster ADH III was observed. Northern blot analysis revealed that B. mon ADH III mRNA is expressed in all tissues from larva examined: fat body, midgut, epidermis, silk gland and ovary, with the highest level found in the fat body.

• YAKHAK HOEJI
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• v.36 no.5
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• pp.469-473
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• 1992

Yeast alcohol dehydrogenase (YADH) has an acidic residue that interacts with the 2'- and 3'-hydroxyl groups of the adenosine ribose of the $NAD^+$ coenzyme. The acidic residue of Asp-223 (according to horse liver alcohol dehydrogenase amino acid sequence) is supposed to determine the coenzyme specificity for $NAD^+$ rather than $NADP^+$. We mutated Asp-223 to leucine and the mutant YADH was expressed in yeast and characterized for the coenzyme specificity. The turnover numbers of mutant enzyme for $NAD^+$ and ethanol were decreased 3.5- and 4.8-fold compared to wild-type enzyme, respectively. Contrastively, catalytic specificity for $NADP^+$ was increased 13-fold. As a result, the mutant YADH also employed $NADP^+$ as a coenzyme.

• Archives of Pharmacal Research
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• v.20 no.2
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• pp.115-121
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• 1997

Ile-269 in horse liver alcohol dehydrogenase isoenzyme S(HLADH-S) was mutated to serine by phosphorothioate-based site-directed mutagenesis in order to study the role of the residue in coenzyme binding. The specific activity of the mutant(1269S) enzyme to ethanol was increased 49-fold. All turnover numbers of 1269S enzyme toward 9 primary alcohols were increased. The mutant enzyme showed 3.6, 4.6, 11.6-fold higher catalytic efficiency for $5{\beta}$-androstane-3, 17-dione, $5{\beta}$-cholanic acid-3-one and retinal than wild-type, respectively. The reaction mechanism of 1269S enzyme was ordered bi bi as wild-type's. These results indicate that the hydrophobic interaction of Ile-269 residue with coenzyme plays an important role in dissociation of coenzyme from enzyme-coenzyme complex, which has been known as the rate limiting step of ADH reaction.