• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.3
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• pp.396-400
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• 2008

The effect of Paecilomyces tenuipes water extract (PTWE) on the alcohol metabolism was examined on rats. PTWE of 0, 30, 100 mg/kg body weight was administrated orally to the rats 30 min before oral treatment of 3 g/kg body weight of alcohol. Blood alcohol and acetaldehyde concentrations were measured 0.5, 1, 3, 6, 9 hr after alcohol treatment. Hepatic alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ADH), microsomal ethanol oxidizing system (MEOS) activities were measured 9 hr after alcohol treatment. There were no differences in blood alcohol concentrations and area under the curve (AUC) of alcohol. PTWE decreased acetaldehyde concentration and there were significant differences after 6 hr in 30 mg/kg PTWE and after 3 and 9 hr in 100 mg/kg PTWE, respectively. In particular, 100 mg/kg PTWE decreased AUC of acetaldehyde by 44%. However, there were no changes in the hepatic ADH, ALDH, and MEOS activities.

• Preventive Nutrition and Food Science
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• v.3 no.4
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• pp.351-355
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• 1998

The purpose of this study was to investigate the effect of protein and dietary fiber levels on the activities of ehanol metabilizing enzymes of the brain in acute and chronic ethanol-treated rats. Male Sprague-Dwley rats were fed on diets containing two levels of protein(7%, 20%)) with two levels of fiber(5%, 105) for 5 weeks. Rats were orally administered 40% (v/v) ethanol(5g/body weight) 90 min before decapitation in the acute ethanol-treated groups and 25% (v/v) ethanol (5g/kg body weight) once a day for 5 weeks in the chronic ethnol-treated groups. Cytosilic alcohol dehydrogenase (ADH) activities were higher than those of mitochondrial ADH. The ADH activities were increased by 20% protein and %% fiber levels in the diet in two fractions , but were decreased by chronic ethanol treatment. Mitochondrial aldehyde dehydrogenase (ALDH) activities did not change by ethanol treatment but were increased by the 20% protein level. However, cytosilic ALDH activities were decreased by chronic ethanol treatment at the 5% fiber level and did not change with protein levels. Both ALDH activities were higher in the 10% fiber groups than the 5% fiber groups. Cytochrome P-450 contents were significantly increased in the chronic ethanol-treated groups but xanthine oxidase (XO) activities did not change. P-450 contents and XO activities were significantly decreased in both the low protein and fiber groups.

• Natural Product Sciences
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• v.1 no.1
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• pp.55-60
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• 1995

In the course of evaluation of hepatoprotective components against alcohol-induced toxicity from Aloe spp., the methanol extract was found to cause a significant inhibition of rat liver cytosolic alcohol dehydrogenase activity. Systematic fractionation of active tractions monitored by bioassay led to isolation of four compounds; aloe-emodin, aloenin, ethylidene-aloenin and ${\beta}-sitosterol$, which were estimated as active principles for inhibition of c-ADH and c-ALDH activities in vitro.

• Food Science and Preservation
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• v.18 no.3
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• pp.407-413
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• 2011

This study was carried out to investigate the effect of a beverage that contained Bulnesia sarmienti(BSP, 2.5%) on rats to which alcohol was administered. The treatment of the BSP group reduced the serum alcohol concentration to 52%, compared to 47% in the positive control(PC) group. Similar pattell1s were observed in the enhancement of alcohol dehydrogenase(ADH), acetaldehyde dehydrogenase(ALDH), alkaline phosphate(ALP), alanine aminotransferase(ALT), asparate aminotransferase(AST), total cholesterol(CHOL), ${\gamma}$-glutamyltrasferase(GGT), glucose(GLU), total bilirubin, and total protein(TP) in the serum. Also, in the BSP group, the lipoxidase(LPO), glutathion-S-transferase(GST), XO, catalase(CAT), and superoxide dismutase(SOD) were significantly reduced, compared to the CO and PC groups in the liver. The glutathione(GSH) activity increased in the BSP group, though. These results indicate that Bulnesia sarmienti extract can enhance alcohol metabolization activity.

• Journal of Life Science
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• v.20 no.5
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• pp.768-774
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• 2010

In this study, we investigated the antioxidant activities, alcohol metabolizing activities, nitrite scavenging ability, angiotensin converting enzyme (ACE), and elastase inhibitory effects of hot water extract from Makgeoly (HWM). Antioxidant activities were measured by using 2,2.diphenyl.1.picryl.hydrazyl (DPPH) free radical scavenging activity and SOD (superoxide dismutase).like activity. The DPPH radical scavenging activity and SOD.like activity of HWM were remarkably increased in a dose.dependent manner and were 48.0% and 98.7% at 10 mg/ml, respectively. To determine the influence of HWM on alcohol metabolizing activity, the generating activities of reduced.nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. The facilitating rates of ADH and ALDH activity by HWM were remarkably increased in a dose.dependent manner and were 70.2% and 64.1% at 10 mg/ml, respectively. The inhibitory activity against angiotensin converting enzyme (ACE) of HWM was increased in a dose.dependent manner and was 74.2% at 10 mg/ml. The nitrite scavenging ability of HWM showed the most remarkable effect at pH 1.2 and 2 mg/ml. These results indicated that HWM may have valuable biological properties owing to their antioxidant activities, ADH and ALDH activity, nitrite scavenging ability, and ACE inhibitory activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.3
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• pp.269-276
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• 1988

식이성 아연이 에탄올의 생체대사율에 미치는 영향을 검토코저 흰쥐에 식이중 아연의 함량(100ppm, 5ppm)을 달리하여 성장시키면서 에탄올을 4주 및 7주간 급여한 다음, 체중증가량과 에탄올의 대사에 관여한다고 알려져 있는 alcohol dehydrogenase, microsomal ethanol oxidizing system, catalase 및 aldehyde dehydrogenase의 활성변동과 혈중 에탄올 제거율을 측정한 결과는 다음과 같다. 실험기간 중 체중증가량은 대조군에 비해 Zn이 부족한 실험군에서 감소되었으며, 에탄올을 투여한 CE군과 ZnDE군은 control에 비해 현저히 감소하였다. Zn 부족한 군(ZnD)에서의 간 ADH, MEOS의 활성 및 혈액중 에탄올 제거율이 아연이 충분히 함유된 대조군에 비해 감소하였으나, catalase와 AIDH의 활성은 별다른 차이를 관찰할 수 없었다. 한편 에탄올을 투여한 CE 및 ZnDE군에서는 대조군(C 및 ZnD)에 비하여 ADH, MEOS 및 혈액중 에탄올 제거율이 증가하였으며 그 증가율은 아연을 충분히 급여한 CE군에서 아연이 부족한 ZnDE 군에 비하여 높게 나타났다. AIDH의 활성은 에탄올의 투여에 의해 CE군에서는 증가하였으나 ZnDE군에서는 별다른 변동을 관찰할 수 없었으며 catalase의 활성은 전실험군에 있어서 차이를 발견할 수 없었다.

• YAKHAK HOEJI
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• v.37 no.6
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• pp.647-658
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• 1993

The susceptibilities of aldehyde dehydrogenase (AldDH) and alcohol dehydrogenase (ADH) to active oxygen generated by xanthine-xanthine oxidase (XOD) system were studied. Incubation of AldDH with 2$\times$10$^{-3}$ units of XOD for 30 min at $25^{\circ}C$ resulted in the decrease of enzyme activity to 30% and it was inactivated completely when incubated with 5$\times$10$^{-3}$ units of XOD. Whereas 70% of ADH activity was retained after exposure to 5$\times$10$^{-3}$ units of XOD for 30 min, 40% of ADH activity was retained after exposure to 5$\times$10$^{-2}$ unit of XOD for 30 min. This inhibition effect by the active oxygen was preventable by catalase and glutathione, but not by SOD. The rates of the NADPH-dependent oxygen consumption by the liver S-9 mixture and microsomes were also determined in this study. Rate of oxygen consumption is increased in the liver S-9 mix and microsomes from phenobarbital-treated rat, and it was consistent with increased lipid peroxidation. In the presense of ethanol as a substrate, the oxygen consumption rates were increased. It is reported that hepatic AldDH activity is depressed in alcoholic liver diseases, however there is few report that explains the reason of depressed AldDH activity. These results are supportive of the theory that the increase in hepatic ethanol oxidation through the induced ME activity after chronic ethanol feeding generate oxygen radical at elevated rates and it leads to the depression of AldDH activity.

• 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.

• Journal of Microbiology and Biotechnology
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• v.14 no.3
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• pp.540-546
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• 2004

We deviced a new graphite-Mn(II) electrode and found that the modified electrode with Mn(II) can catalyze NADH oxidation and $NAD^+$ reduction coupled to electricity production and consumption as oxidizing agent and reducing power, respectively. In fuel cell with graphite-Mn(II) anode and graphite-Fe(III) cathode, the electricity of 1.5 coulomb (A x s) was produced from NADH which was electrochemically reduced by the graphite-Mn(II) electrode. When the initial concentrations of pyruvate and acetaldehyde were adjusted to 40 mM and 200 mM, respectively, about 25 mM lactate and 35 mM ethanol were produced from 40 mM pyruvate and 200 mM acetaldehyde, respectively, by catalysis of ADH and LDH in the electrochemical reactor with $NAD^+$ as cofactor and electricity as reducing power. By using this new electrode with catalytic function, the bioelectrocatalysts are engineered; namely, oxidoreductase (e.g., lactate dehydrogenase) and $NAD^+$ can function for biotransformation without electron mediator and second oxidoreductase for $NAD^+$/NADH recycling.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.3
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• pp.173-178
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• 2001

Food yeast, Saccharomyces cerevisiae, is a safe organism with a long history of use for the production of biomass rich in high quality proteins and vitamins. AmA1, a seed storage albumin from Amaranthus hypochondriacus, has a well-balanced amino acid composition and high levels of essential amino acids and offers the possibility of further improving food animal feed additives. In order to find an effective means of expressing AmA1 in yeast, the gene was cloned into an episomal shuttle vector. Four different promoters were tested: the glyceraldehyde-3-phosphate dehydrogenase promoter, galactose dehydrogenase 10 promoter, alcohol dehydrogenase II promoter, and a hybrid ADH2-GPD promoter. The recombinant AmA1 genes were then introduced into the yeast Saccharomyces cerevisiae 2805. Northern and Western blot analyses of the yeast under appropriate conditions revealed that AmA1 was expressed by all four promoters at varying levels. An enzyme-linked immunosorbent assay demonstrated that the amount of AmA1 protein in the recombinant yeast was 1.3-4.3% of the total soluble proteins. The highest expression level was obtained from the hybrid ADH2-GPD promoter.