• 제목/요약/키워드: acetaldehyde dehydrogenase (ALDH)

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감과 가공식품의 알콜대사촉진물질 (Acetaldehyde Dehydrogenase Activator from Persimmon and Its Processed Foods)

  • 김석기;이영철;서광기;최혜선
    • 한국식품영양과학회지
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    • 제30권5호
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    • pp.954-958
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    • 2001
  • 감은 종기, 염증질환, 부스럼 화상을 치료하고 고혈압을 예방하고 동맥경화에 효과가 있고 숙취해소에 효능이 있다고 알려져있다. 감과육에 알콜대사에 관여하는 acetaldehyde dehydrogenase(ALDH)의 활성을 촉진하는 물질이 존재하므로ALDH의 활성을 촉진하는 물질을 감의 계절별, 품종별 측정을 했고 또 감을 이용한 가공식품에 농도를 측정하였다. ALDH의 활성을 촉진하는 물질은 부유의 경우 11월에 수확한 과일에서 가장 높고 품종별로는 부유가 가장 높았고 갑주백목은 부유와 유사하였고 청도반시, 서촌조생의 순이었다. 가공식품은 감건조품, 곶감, 감즙은 대체로 ALDH의 활성을 촉진하는 물질의 활성이 높게 유지되나 감음료, 감식초와 같은 음료는 ALDH의 활성을 촉진하는 물질의 활성이 낮았다. 감 자체뿐만 아니라 감가공식품에서도 ALDH의 활성을 촉진하는 물질의 활성이 어느 정도 유지되므로 이를 이용한 숙취해소작용이 기대된다.

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알데히드 탈수소 효소 활성에 미치는 글루타치온의 영향 (Effect of Glutathione on Aldehyde Dehydrogenase Activity)

  • 이은실;문전옥
    • Environmental Analysis Health and Toxicology
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    • 제16권1호
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    • pp.9-16
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    • 2001
  • It is known that alcoholics have significantly lower mitochondrial aldehyde dehydrogenase (ALDH)s'activity than do normal subjects or nonalcoholics with liver disease. However, there are only few reports that explain the reasons behind this reduction of ALDHs'activities. In this study, ALDH activity is inhibited by acetaldehyde, a substrate for ALDH However, the addition of glutathione (GSH) protected ALDH activities against the inhibitory effects of acetaldehyde in vitro. Furthermore, when GSH depletion is induced using diethyl maleate (DEM) in rats by 24% in cytosol and 43% in mitochondria, ALDH activities were also depressed by 31% and 63%, respectively compared to non-treated rats without significant reductions in other hepatic enzymes. These results suggest that ALDHs'activities are closely related to the concentration of acetaldehyde and/or cellular GSH contents . Therefore in alcoholic liver disease, increased productions of acetaldehyde and decreased contents of mitochondrial GSH may involved in the depression of ALDHs'activities.

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Expression of Human Mitochondiral Aldehyde Dehydrogenase 2 in Mammalian Cells using Vaccinia Virus-T7 RNA Polymerase

  • Kang, Su-Min;Yoo, Seung-Ku;Lee, Ki-Hwan
    • Journal of Microbiology
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    • 제37권1호
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    • pp.41-44
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    • 1999
  • Human mitochondrial aldehyde dehydrogenase 2 (ALDH2) is mainly responsible for oxidation of acetaldehyde generated during alcohol oxidation in vivo. A full-length cDNA of human liver ALDH2 was successfully expressed using a vaccinia virus-T7 RNA polymerase system. The expressed ALDH2 had an enzymatic activity as high as the native human liver ALDH2 enzyme.

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약용식물 추출물의 에탄올대사 효소활성에 미치는 영향 (Effect of Medicinal Plant Extracts on the Ethanol-Metabolizing Enzyme Activities)

  • 도재호;곽정원;이선정;노정진;이광승;김동청
    • 산업식품공학
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    • 제21권3호
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    • pp.286-291
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    • 2017
  • 약용식물의 열수 추출물이 in vitro에서 alcohol dehydrogenase (ADH)와 aldehyde dehydrogenase (ALDH)의 활성에 미치는 영향을 확인하였다. 약용식물에 20배의 증류수를 넣고 $80^{\circ}C$에서 8시간 추출하여 얻어진 추출액을 시료로 사용하였다. 50종의 약용식물 중에서 마늘과 육계 추출물이 숙취해소 천연소재로서의 활용 가능성이 가장 높게 나타났다. 마늘 추출물은 ADH에 비해 ALDH의 활성을 2배 이상 촉진시킴으로써 acetaldehyde의 분해가 잘 되게 하였다. 육계 추출물은 ALDH의 활성에 비해 ADH의 활성을 획기적으로 저해함으로써 acetaldehyde의 생성을 크게 억제하였다. 육계 추출물은 농도에 비례하여 ADH와 ALDH의 활성을 저해하였으며, $45.33{\mu}g/mL$의 농도에서 ADH의 활성을 52.8% 저해하였고 ALDH의 활성을 11.0% 저해하였다.

바이오짐의 에탄올 대사에 대한 영향 (Effects of Biozyme on the Ethanol Metabolism in vivo and in vitro)

  • 남석우;박승희;윤성필;서동완;남태균;홍성렬;이향우
    • Biomolecules & Therapeutics
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    • 제3권2호
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    • pp.171-175
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    • 1995
  • Effects of $Biozyme_{R}$ and $\textrm{Business}_{R}$ on alcohol metabolism in rats, and on the activities of alcohol dehydrogenase(ADH) and acetaldehyde dehydrogenase(ALDH) were studied in vitro. Alcohol concentration in rat blood was decreased after the treatment of Business(3.3 mι/kg, Biozyme 1.67 mg/wι) and Biozyme(3.3 mι/kg, 1.67 mg/mι) prior to the administration of ethanol(25%, 0.83 g/kg). And the acetaldehyde concentration of rat blood was also decreased when compared with control values in the same condition. Effects of Biozyme on ADH and ALDH activity were also studied. While the ALDH activity was elevated in the presence of Biozyme(2 $\mu\textrm{g}$/assay), the ADH activity was not influenced by Biozyme at the concentration range from 2 $\mu\textrm{g}$/assay to 0.2 mg/assay. In summary, Biozyme accelerated the rate of ethanol metabolism and the acceleration might be due to the increase in ALDH activity.vity.

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Purification of Mitochondrial Matrix Aldehyde Dehydrogenase from Pig Brain

  • Kim, Kyu-Tae;Lee, Young-Don
    • BMB Reports
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    • 제28권2호
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    • pp.177-183
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    • 1995
  • The activity of aldehyde dehydrogenase (ALDH) in the cerebrum, cerebellum, striatum, and medulla oblongata was examined and mitochondrial matrix ALDH was purified prior to immunohistochemical study on the localization of ALDH isozymes in pig brain. Relatively high enzyme activity was found in the striatum and medulla oblongata when using indole-3-acetaldehyde as substrate, and in the striatum when using 3,4-dihydroxyphenylacetaldehyde (DOPAL). The main part of mitochondrial ALDH activities with both acetaldehyde and DOPAL existed in the matrix fraction. The ratio of activity of the matrix to the membrane fraction in the cerebrum was higher than in the cerebellum, suggesting that the distribution pattern of ALDH isozymes was different according to the brain regions. The 276-fold purified mitochondrial matrix ALDH from pig brain was identified to be homologous tetramers with 53 KD subunits. The enzyme showed maximal activity at pH 9.0 and was stable in the temperature range from $25^{\circ}C$ to $37^{\circ}C$. The mitochondrial matrix ALDH activity was considerably inhibited by acetaldehyde in vitro. The $K_m$ values of the enzyme for acetaldehyde and propionaldehyde were 5.8 mM and 4.9 mM, respectively, whereas $K_m$ values for indole-3-acetaldehyde and DOPAL were 44 ${\mu}M$ and 1.6 ${\mu}M$, respectively. The $V_{max}/K_{m}$ ratio was the highest with DOPAL as compared with other substrates. These results suggested that mitochondrial matrix ALDH in the present work might be a low Km isozyme involved in biogenic aldehyde oxidation in pig brain.

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인삼사포닌 분획이 에탄올을 투여한 쥐의 뇌에서 분리한 신경세포와 Astrocyte의 Aldehyde Dehydrogenase 활성에 미치는 영향 (The Effect oi Saponin Fraction of Panax Ginsen C.A. Meyer on Aldehyde Dehydrogenase Activity in Neurons and Astrocytes Isolated from Ethanol Administered Rat Brain)

  • 이명돈;황우섭;서해영
    • Journal of Ginseng Research
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    • 제21권1호
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    • pp.53-60
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    • 1997
  • The changes in aldehyde dehydrogenase(ALDH, E.C. 1.2.1.3.) activity in neurons and astrocytes isolated from rat brains were investigated after administration of ethanol and Korean red ginseng(Panax ginseng C.A. Meyer) saponln. The cerebral ALDH activity with acetaldehyde and Propionaldehyde was higher in the white matter than in the gray matter. However, using indole-3-a-cetaldehyde and 3,4-dihydroxyphenylacetaldehyde as substrates, there was no significant difference in activity between two regions in cerebrum. In ethanol treated group, ALDH activity with all the substrates in the gray and white matter was lower than in normal group. In ethanol-saponin treated group, the enzyme activity in the white matter remarkably Increased. The ALDH activity in neurons isolated from cerebral cortex in ethanol-treated group was lower than in normal group. In ethanol-saponin treated group, neuronal ALDH activity with propionaldehyde was significantly recovered but not with Indole-3-acetaldehyde. In astrocytes, although the ALDH activity with propionaldehyde in the ethanol-treated group was not changed as compared with normal group, considerable increase in activity was found in ethanol-saponin treated group. These results suggest that Korean red ginseng saponin may protect the neuronal functions from the toxic effects of acetaldehyde derived from ethanol by stimulation of ALDH activity in astrocytes surrounding nerve cells.

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Effect of Fermented Sea Tangle on the Alcohol Dehydrogenase and Acetaldehyde Dehydrogenase in Saccharomyces cerevisiae

  • Cha, Jae-Young;Jeong, Jae-Jun;Yang, Hyun-Ju;Lee, Bae-Jin;Cho, Young-Su
    • 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.

알코올 대사 효소 alcohol dehydrogenase (ADH) 및 acetaldehyde dehydrogenase (ALDH) 활성에 미치는 아미노산의 영향 (Effects of Amino Acids on the Activities of Alcohol Metabolizing Enzyme Alcohol Dehydrogenase (ADH) and Acetaldehyde Dehydrogenase (ALDH))

  • 차재영;정해정;정재준;양현주;김용택;이용수
    • 생명과학회지
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    • 제19권9호
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    • pp.1321-1327
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    • 2009
  • 본 연구에서는 숙취해소에 좋은 것으로 알려진 식품 소재의 주요 아미노산을 포함하여 효소 활성에 영향을 미치는 것으로 알려진 아미노산을 선택하였고, 효소 활성도가 상대적으로 높은 yeast와 rat liver 유래의 ADH 및 ALDH 효소를 대상으로 알코올 대사에 관련된 효소 활성의 촉진 효과에 대하여 검토하였다. Rat liver 유래의 ADH 활성은 처리한 아미노산 중에서 arginine에서 가장 높았다. Arginine의 첨가 농도를 달리하여 효소 활성을 측정한 결과 $10{\sim}50\;mg$/ml 농도에서 $118{\sim}120.6%$로 양성대조구의 90.6% 보다 약간 높은 것으로 나타났다. 또한, yeast 유래의 ADH 활성은 methionine에서 가장 높은 활성을 보였고, methionine의 처리 농도를 달리한 경우에서는 첨가 농도 의존적으로 높은 활성을 보였다. Rat liver 유래의 ALDH 활성은 methionine이 가장 높은 활성을 보였다. Methionine의 첨가 농도별 측정에서는 10 mg/ml에서 30 및 50 mg/ml 첨가 농도에서 보다 높은 활성을 보였으며, 이들 모든 처리 농도에서 양성대조구 보다 상당히 높은 활성을 보였다. 한편 yeast 유래의 ALDH 활성은 각 아미노산별 큰 차이는 없었으나, arginine에서 높은 활성을 보였다. Arginine의 첨가 농도별 측정에서는 처리 농도 의존적으로 활성이 약간씩 증가하는 경향을 보였으며, 양성대조구 보다 높은 활성을 나타내었다. 효모 유래 ALDH 및 rat liver 유래 ADH 효소 활성을 촉진시키는 작용을 가진 arginine을 효모 배양에 첨가시킬 경우 세포 내 ALDH 및 ADH 활성 염색 정도가 증가함으로써 arginine은 ALDH 및 ADH 활성을 촉진시키는 효능이 in vivo 실험계에서도 확인되었다. 이상의 실험 결과에서 아미노산 중에서는 arginie과 methionine이 ADH 및 ALDH 활성을 촉진시키는 작용에 의해 알코올 분해뿐만 아니라 acetaldehyde의 분해도 촉진시킬 가능성이 높아 숙취해소 효과는 물론 간 보호 효과도 동시에 있을 것으로 시사 되어 진다. 따라서 arginine과 methionine과 같은 아미노산을 주류 제품에 첨가하게 될 경우 숙취해소 경감과 간 보호 효능을 어느 정도 나타낼 수 있을 가능성이 제기되었다.

랫드에서 Aldehyde Dehydrogenase Related Compounds의 알콜 및 알데히드 분해 효능평가 (Anti-Alcohol and Anti-Aldehyde Hangover Effect of Aldehyde Dehydrogenase Related Compounds in Rat)

  • 신혜정;정세영;강소라;권흥택;김배환
    • 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.