• 한국식품영양과학회지
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• 제30권4호
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• pp.679-683
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• 2001

본 실험은 알코올 투여한 흰쥐를 대상으로 콩나물, 솔잎, 표고버섯과 오가피 추출물의 알코올 탈수소효소 활성과 항산화 효과를 비교하기 위해 수행되었다. 약 200g 정도의 Sprague-Dawley계 쥐들을 정상군, 알코올 단독투여군, 4가지 식물추출물 투여군으로 나우어서, 각 식물추출물을 알코올을 주입하기 전 8일 동안 200mg/kg b.w. 을 하루에 한번 경구투여하였다. 모든 동물은 알코올을 주입하고 90분 후에 도살시켰다. 콩나물과 솔잎추출물 투여군의 혈중 알코올 농도는 알코올 단독투여군, 표고버섯, 오가피군 보다 유의적으로 낮게 나타났다. 또한 콩나물과 솔잎 추출물 투여군의 알코올 탈수소효소활성은 알코올 단독투여군과 표고버섯, 오가파군보다 유의적인 증가를 보여주었다. Catalase 활성은 식물추출물 투여군이 알코올 단독투여군보다 다소 높게 나타났지만, 유의성 있는 차이는 보이지 않았다. 이러한 결과는 흰쥐에게 일회성으로 알코올을 다량 투여했을 때 알코올 탈수소효소가 catalase보다 우선적으로 알코올 대사에 반응함을 보여준다. 모든 식물추출물 투여군들의 지질과산화와 glutathione peroxidase 활성은 알코올 단독투여군보다 유의적으로 낮게 나타났다. 이 결과는 본 실험에 사용된 식물추출물들이 알코올의 산화에 대한 항산화 효과를 가진다는 것을 보여주며, 특히 콩나물과 솔잎 추출물 투여군이 알코올 탈수소효소의 활성증가오 항산화에 대한 효과가 높음을 보여주었다.

• Journal of Microbiology and Biotechnology
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• 제21권8호
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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.

• 한국식품저장유통학회지
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• 제15권1호
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• pp.155-160
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• 2008

본 연구는 대구 무형문화재 제11호인 하향주의 품질 우수성을 규명하고자 향기성분 분석 후 랫드에 대한 알코올 대사 특성을 조사하였다. GC/MS 분석시, 하향주는 iso-butyl alcohol과 iso-amyl alcohol 등을 포함하여 17가지의 향기성분이 분석되었고 여과에 의해 acetaldehyde와 ethylacetate의 농도는 낮아짐을 확인하였다. 하향주와 동일한 농도인 17% 알코올을 SD계 랫드에 단회 경구 투여시 혈중 알코올 농도와 acetaldehyde 농도가 하향주 투여군이 낮았으며, 5시간 뒤 간조직에서 alcohol dehyogenase와 acetaldehyde dehyogenase의 농도는 하향주 투여군이 17% 알코올 투여군보다 높았다. 따라서 하향주는 동일농도의 17% 알코올 투여군보다 알코올 대사를 촉진시켜 숙취를 감소시킴을 확인하였다.

• 한국식품위생안전성학회지
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• 제30권1호
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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.

• 한국수산과학회지
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• 제43권1호
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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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• 제7권3호
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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.

• 한국환경보건학회지
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• 제49권2호
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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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• 제7권1호
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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.

• 약학회지
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• 제36권5호
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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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• 제20권2호
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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.