• Title/Summary/Keyword: dehydrogenease

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

  • 김석기;이영철;서광기;최혜선
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.30 no.5
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    • pp.954-958
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    • 2001
  • Perismmon has been consumed for long times in Korea and used as a drug for a long time in Korea, It was known to help alcohol intoxication. Ingested alcohol is metabilized by alcohol dehydrogenease and acetaldehyde dehydrogenase in liver. Alcohol dehydrogenease activator and acetaldehyde dehydrogenase activator(ALDHA) was detercted in persimmon. The oncentration of ALDHA was determined and compared in different havesting time, species, and available processed foods. The level of ALDHA was highest in persimmon (Fuyu) harvested in November. Lower ALDHA activities were found in its processed foods. Persimmon and its processed foods are expected to be effective in decreasing the concentration of alcohol and acetaldehyde after alcohol intake.

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Alcohol Metabolizing Activity of Fermented Sea Tangle Juice (Lactobacillilus brevis를 이용한 다시마 발효물의 알코올 분해 활성)

  • Kang, Young-Mi;Lee, Bae-Jin;Kim, Jin-Su
    • 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.

Some Properties of Xanthine Dehydrogenase from Pseudomonas synuantha A3 (Pseudomonas synxantha A3에서 분리한 Xanthine Dehydrogenase의 성질)

  • 전흥기;사까이다꾸오
    • Microbiology and Biotechnology Letters
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    • v.19 no.6
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    • pp.610-613
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    • 1991
  • Some of the Kinetic properties of crystallic xanthine dehydrogenase form Pseudomonas synxantha A3 were studied. The enzyme activity was strongly inhibited by adenine, 8-azaadenine, 2-methyladenine, guanine, and 8-azaguanine, but not by caffeine, and the inhibitions by adenine and guanine were observed to be of noncompetitive type. The $K_i$ values for adenine and guanine were 0.037 and 0.098 mM, respectively. Michaelis constants were found to be 0.33 and 0.06 rnM for hypoxanthine and xanthine with $NAD^+$ as the second substrate, respectively, and 0.1 rnM for $NAD^+$ with either hypoxanthine or xanthine as the second substrate.

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