• 제목/요약/키워드: Alcohol dehydrogenase (ADH)

검색결과 220건 처리시간 0.033초

Elucidation of the Regulation of Ethanol Catabolic Genes and ptsG Using a glxR and Adenylate Cyclase Gene (cyaB) Deletion Mutants of Corynebacterium glutamicum ATCC 13032

  • Subhadra, Bindu;Lee, Jung-Kee
    • Journal of Microbiology and Biotechnology
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    • 제23권12호
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    • pp.1683-1690
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    • 2013
  • The cyclic AMP receptor protein (CRP) homolog, GlxR, controls the expression of several genes involved in the regulation of diverse physiological processes in Corynebacterium glutamicum. In silico analysis has revealed the presence of glxR binding sites upstream of genes ptsG, adhA, and ald, encoding glucose-specific phosphotransferase system protein, alcohol dehydrogenase (ADH), and acetaldehyde dehydrogenase (ALDH), respectively. However, the involvement of the GlxR-cAMP complex on the expression of these genes has been explored only in vitro. In this study, the expressions of ptsG, adhA, and ald were analyzed in detail using an adenylate cyclase gene (cyaB) deletion mutant and glxR deletion mutant. The specific activities of ADH and ALDH were increased in both the mutants in glucose and glucose plus ethanol media, in contrast to the wild type. In accordance, the promoter activities of adhA and ald were derepressed in the cyaB mutant, indicating that glxR acts as a repressor of adhA. Similarly, both the mutants exhibited derepression of ptsG regardless of the carbon source. These results confirm the involvement of GlxR on the expression of important carbon metabolic genes; adhA, ald, and ptsG.

Acetobacter sp. CS5 Alcohol Dehydrogenase의 분리 및 특성 (Purification and Characterization of Alcohol Dehydrogenase from Acetobacter sp. CS5)

  • 김춘성;송규영;김성준;김호상;박현균;이숙영;박종필
    • KSBB Journal
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    • 제14권5호
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    • pp.528-533
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    • 1999
  • 초산생성 미생물인 분리균주 Acetobacter sp. CS5로부터 alcohol dehydrogenase(ADH)를 순수분리하였다. 이 효소는 Triton-X로 solubilization시킨 후 DEAE-Sephacel chromatography와 Sephacryl S-200 chromatography에 의해서 순수 분리되었다. 그 결과 15%의 수율과 14배의 정제된 효소를 얻었다. 정제된 효소의 분자량은 322 KDa으로 측정되었다. 또한 SDS-PAGE상에서는 분자량이 79 KDa, 49 KDa, 46KDa인 3개의 band를 확인하였고, 3분자의 79 KDa 소단위체와 각각 1분자인 49 KDa과 46 KDa인 소단위체로 이루어졌음을 확인하였다. 에탄올에 대한 Km값은 0.77 mM이었으며 최적 pH와 온도는 각각 4.0~5.0과 35$^{\circ}C$이였다.

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Acetobacter sp. HA로부터 Membrane-bound Alcohol Dehydrogenase의 정제 및 특성 (Purification and Properties of a Membrane-bound Alcohol Dehydrogenase from Acetobacter sp. HA)

  • 유진철;심정보;김형근;전홍성;김성준
    • 미생물학회지
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    • 제32권1호
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    • pp.78-83
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    • 1994
  • 초산 생성 균주인 Acetobacter sp. HA로부터 membrane-bound alcohol dehydrogenase(ADH)를 분리 정제하였다. 세포막 분획과 세포막에서 효소의 용출 그리고 크로마토그라피 방법 등을 적용하여 수율 35%, 153배 정제된 효소를 획득하였다. 정제된 효소의 분자량은 330,000 dalton이었으며, 각각 분자량 79,000과 49,000 그리고 45,000 dalton을 가진 세 종류의 subunit로 이루어져 있었다. 그리고 흡수 스펙트럼의 분석 결과 본 효소에는 cytochrome c가 존재함을 확인할 수 있었다. 본 효소는 메탄올을 제외한 1차 지방족 알코올을 기질로 이용할 수 있었으며, formaldehyde, acetaldehyde 그리고 glutaraldehyde의 경우에도 다소간 기질로 이용될 수 있었다. 본 효소의 에탄올에 대한 $K_m$값은 1.38mM이었으며, 최적 pH와 온도는 각각 5.0~6.0과 32${\circ}C$이었다. 본 효소의 활성은 $V_2O_5$$ZnCl_2,\; NiCl_2$같은 금속 이온에 의하여 저해되었다.

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Pseudomonas 속균이 생산하는 Alcohol Dehydrogenase에 관한 연구 (제1보) Alcohol Dehydrogenase 정제와 일반적성질 (Alcohol Dehydrogenase Active on Furfuryl Alcohol from Pseudomonas sp. (Part 1) Purification and Properties of Alcohol Dehydrogenase)

  • 강순선
    • 한국미생물·생명공학회지
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    • 제8권1호
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    • pp.27-32
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    • 1980
  • 본 실험에서 얻은 성과를 요약하면 다음과 같다. \circled1 Furfuryl alcohol를 단일탄소원으로 이용하여 ADH를 생산하는 세균을 토양중에서 분리하고, 균학적 성질에 따라 Pseudomonas sp.라 동정하였다. \circled2 본 효소는 disc 전기영동적, SDS 전기영동적, 초원침강적, 분석에서 완전히 균일하였다. \circled3 본 효소의 침강계수는 7.6S, 반응최적활성 pH는8.5~9.0에 위치하였으며, 최적활성온도는 45$^{\circ}C$ 이었다. \circled4 4개의 동일 subunit (M.W 30,000)가 회합하여 본 활성효소를 형성하는 tetramer이며, 분자량은 개략 120,000이다. \circled5 본 효소의 subunit 1분자는 266개의 amino 산 residues로 구성되고 있다.

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발효한약추출물 HP-1이 알코올을 투여한 쥐의 알코올 대사에 미치는 영향 (Effect of Fermented Herbal Extracts, HP-1 on Enzyme Activities and Gene Expressions Related to Alcohol Metabolism in Ethanol-loaded Rats)

  • 정용준;한동오;최보희;박철;이혜정;김성훈;함대현
    • 동의생리병리학회지
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    • 제21권2호
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    • pp.387-391
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    • 2007
  • Recently, much attention has been paid to developing various kinds of fermented herbal extracts, a new type of traditional herbal medicine, in the field of Korean traditional medicine. The fermentation of medicinal herbs is intended to exert a favorable influence on digestability, bioavailavility and pharmacological activity of herbal extract in the gastrointestinal tract. It also produces a number of fermentation products that intensify the nutritional and pharmacological aspects of the medicinal herbs. In order to develop a functional beverage of alleviating the aftereffects of the previous drinks, the extracts (HP-1) of fermented herbal mixture, including Artemisia capillaris Thunb., Lonicera japonica Thunberg, and Hovenia dulcis Thunb., were prepared and the medicinal effect as a hangover cure was evaluated in ethanol-loaded rats. The enzyme activities of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase-2 (ALDH2) were analyzed by measuring the concentration of blood ethanol and acetaldehyde. The mRNA expression of ADH and ALDH2 was also investigated through RT-PCR analysis. In the HP-1-treated group, the concentration of blood ethanol was significantly reduced at one hour after loading of ethanol, as compared to that in the saline-treated group. The reduced ethanol was converted to acetaldehyde, which resulted in rapid increase in acetaldehyde concentration in an hour. Acetaldehyde was started to decrease at 5 hours after ethanol loading. It implies that HP-1 is highly effective to stimulate the activities of ADH and ALDH2. The HP-1 treatment also activated the mRNA expression of ADH and ALDH. This study suggests that fermented herbal extract, HP-1 can be used as a functional beverage of alleviating the alcohol-induced hangover symptoms by stimulating the activities and gene expression of hepatic alcohol metabolizing enzymes.

무화과(Fig) 효소를 첨가한 유산균을 이용하여 알코올 대사활성 함유 치즈의 제조 (Production of cheese containing alcohol metabolism using Lactobacillus with fig enzyme)

  • 이성재;양영헌;전종민;이기원;조인재;이성민;류정열;신원성;김정수
    • 한국식품과학회지
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    • 제49권2호
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    • pp.141-145
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    • 2017
  • 본 연구에서는 알코올 분해능이 높은 기능성 치즈를 제조하기 위하여 L. kitasatonis, L. amylophillus, L. mesenteroides sub. 및 무화과 효소를 이용하였다. 각각 균주의 에탄올, 내산 및 내담즙에 내성이 우수함을 확인하였고, ADH 및 ALDH 활성도를 측정한 결과 10%의 무화과 효소를 첨가하였을 때의 ADH 활성도는 각각 $688.39{\pm}51.63$, $1054.98{\pm}79.12$, $825.28{\pm}61.89{\mu}mol$로 나타났으며 ALDH는 각각 $751.91{\pm}54.14$, $1209.93{\pm}87.11$, $891.09{\pm}64.16{\mu}mol$로 무화과를 첨가하지 않았을 때보다 각각 증가하는 것으로 나타났다. 또한 L. amylophillus 균주를 이용하여 치즈를 제조한 뒤, 10%의 무화과 효소를 첨가하였을 때 ADH 및 ALDH 분해능이 무화과효소를 첨가하지 않았을 때 보다 각각 252, 246% 증가함을 확인하였다. 결론적으로 무화과 효소를 첨가하였을 때, L. amylophillus을 이용한 치즈의 제품이 높은 알코올 분해능을 가지는 것으로 확인되었고, 이를 통해 기능성 식품의 제조로써 무화과 효소의 적용 가능성을 확인하였다.

레몬 머틀 잎 추출물의 Hep G2 세포에서의 간 보호 효과 및 알코올대사 효소활성 (The Hepatoprotective Effects of Hep G2 Cells and the Alcohol-Metabolizing Enzyme Activities of Lemon-Myrtle (Backhousia citriodora) Leaf Extracts)

  • 정경임;김판길;갈상완;최영주
    • 생명과학회지
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    • 제27권11호
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    • pp.1262-1268
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    • 2017
  • 본 연구에서는 레몬 머틀 잎 열수 및 에탄올 추출물의 새로운 소재로서의 가능성을 검토하고자 항당뇨 효과와 미백 효과, 알코올 분해능 및 간세포 보호 효과를 확인하였다. 레몬 머틀 추출물의 혈당강하효과는 ${\alpha}$-glucosidase 활성 억제능을 측정하였으며, 열수 및 에탄올 추출물 1 mg/ml 농도에서 각각 7.66%와 40.29%로 에탄올 추출물이 높게 나타났고(p<0.05), tyrosinase 저해활성은 에탄올 추출물 1 mg/ml 농도에서 38.26%로 나타났다. 숙취 해소능을 알아보기 위해 alcohol dehydrogenase (ADH) 및 acetaldehyde dehydrogenase (ALDH) 활성을 측정한 결과, 두 효소 모두 레몬 머틀 열수 및 에탄올 추출물의 농도 의존적으로 증가하였다(p<0.05). 레몬 머틀 열수 및 에탄올 추출물은 tacrine으로 유도된 Hep G2 간암 세포주에 대하여 유의적인 보호 활성이 나타났다. 이상의 결과에서와 같이 레몬 머틀 잎은 항당뇨효과와 숙취 해소효과 및 간세포 보호 효과가 있는 것으로 나타났기에 기능성 소재로서의 활용 가능성을 확인할 수 있었다.

오디 추출물의 알코올 분해능 및 항산화 효과 (Study on the Alleviation of an Alcohol Induced Hangover and the Antioxidant Activity by Mulberry Fruit)

  • 이은주;배지현
    • 한국식품영양학회지
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    • 제24권2호
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    • pp.204-209
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    • 2011
  • 본 연구에서는 식용 가능한 오디를 용매별로 추출하여 항산화 효과 및 숙취 해소 활성능을 알아보고자 하였다. 오디Fig. 1. Contents of ADH ability of each solvent fraction of mulberry fruit extract. 추출물에 들어있는 총 페놀 함량을 정량하였으며, 오디 추출물의 전자공여능, SOD 유사 활성, TBARS 아질산염 소거능 등을 통하여 오디의 항산화 활성을 측정하였고, 알코올 분해능은 alcohol dehydrogenase activity assay 방법을 이용하여 조사하였다. 오디 추출물의 총 페놀 화합물은 60% methanol 추출물에서 가장 높게 나타났다. 전자공여능(EDA)은 오디의 40% ethanol 추출물에서 BHT와 유사한 활성을 나타났고, SOD 유사 활성은 BHT보다 오디 추출물이 낮은 활성을 나타내었다. 아질산염 소거능은 오디의 60% ethanol과 40% methanol 추출물이 각각 98%, 97%로 ascorbic acid와 상응하는 결과를 보였다. 알코올 분해능에서는 오디의 60% ethanol 추출물이 가장 높은 활성을 나타내었다.

Effect of alcohol dehydrogenase 1C (ADH1C) genotype on vitamin A restriction and marbling in Korean native steers

  • Peng, Dong Qiao;Jung, U Suk;Lee, Jae Sung;Kim, Won Seob;Jo, Yong Ho;Kim, Min Jeong;Oh, Young Kun;Baek, Youl Chang;Hwang, Seong Gu;Lee, Hong Gu
    • Asian-Australasian Journal of Animal Sciences
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    • 제30권8호
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    • pp.1099-1104
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    • 2017
  • Objective: This work was to find the correlation of alcohol dehydrogenase 1C (ADH1C) genotype with vitamin A reduction and carcass traits during the vitamin A restriction period. Methods: In study 1, 60 Korean native steers were fed a diet (890 IU/kg) with 8,000 IU and 0 IU of supplemental premix vitamin A/kg of dry matter (DM) for control and treatment group, respectively. The levels of serum vitamin A were analyzed through high preparative performance liquid chromatography, and the ADH1C genotype was analyzed based on polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP; 78.1% TT type, 21.9% TC type); however, CC type was not found. Then, the interaction between ADH1C and carcass traits on the vitamin A restriction was investigated in study 2. A total of 136 Korean native steers were fed a diet that included 930 IU/kg vitamin A of DM. Results: Serum vitamin A in treatment was reduced to 112.4 IU/dL in steers with TT type of ADH1C, while for steers with TC type the concentration of serum vitamin A was dropped to 79.5 IU/dL (p<0.1) in study 1. This showed that TC type had the potential to lower serum vitamin A concentration during vitamin A restriction compared to TT type. In study 2 we found that eye muscle area, marbling and carcass weight in Korean native steers with TC type were higher than in steers with TT type (p<0.05). Conclusion: The interaction between vitamin A restriction and TC type of ADH1C gene could have the potential of increasing the marbling in Korean native steers. These results indicated that steers with TC type of the ADH1C gene were more sensitive to the change of serum vitamin A than TT types. Furthermore, this finding has the potential to enable a higher marbling score under the condition of vitamin A restriction in Korean native steers.

Effect of cordycepin-enriched Cordyceps militaris L. extract powder on alcohol degradation and hepatoprotection in mice alcohol model

  • Ju-Hye Kim;Heejin Park;Mun-Hyoung Bae;Youngha Seo;Eun-Young Gu;Taek-Keun Oh;Byoung-Seok Lee
    • 농업과학연구
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    • 제51권2호
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    • pp.169-178
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    • 2024
  • Cordyceps militaris L. (C. militaris) has been traditionally used as tonic medicine for metabolic syndrome. Cordycepin, has been reported with immunomodulatory, antitumor, and hepatoprotective effect, is the main extract from C. militaris. This study was conducted to evaluate the alcohol degradation and hepatoprotective effect of cordycepin-enriched C. militaris extract (CM) powder in chronic and binge ethanol (ethanol Lieber-DeCarli diet)-fed male C57BL/6 Mice. Cordycepin-enriched C. militaris extract powder was orally administered once daily at dose levels of 0, 125, 250, and 500 mg·kg-1·day-1 for 16 days. For evaluating alcohol degradation, ethanol concentration and alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activity were measured in serum. Serum ethanol (EtOH) concentration was decreased at CM treated groups, and the activities of ADH and ALDH were increased dose-dependently at CM treated groups compare to EtOH model group. In clinical chemistry, the values of aspartate aminotransferase (AST) and alanine aminotransferase (ALT) were lower in CM treated groups than those in EtOH model group. Additionally, absolute and relative (to body weight) liver weights were statistically decreased in the CM treated groups compared to the EtOH model group. In conclusion, our study showed that cordycepin-enriched C. militaris extract powder exhibits hepatoprotective effect by upregulating the ADH and ALDH enzyme in an alcoholic liver disease model.