• Title/Summary/Keyword: alcohol-oxidase

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Enzyme Activities Related to the Methanol Oxidation of Mycobacterium sp. strain JCl DSM 3803

  • Youngtae Ro;Kim, Eungbin;Kim, Youngmin
    • Journal of Microbiology
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    • v.38 no.4
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    • pp.209-217
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    • 2000
  • Mycobacterium sp. strain JCl DSM 3803 grown in methanol showed no methanol dehydrogenase or oxidase activities found in mast methylotrophic bacteria and yeasts, respectively. Even though the methanol-grown cells exhibited a little methanol-dependent oxidation by cytochrome c-dependent methanol dehydrogenase and alcohol dehydrogenase, they were not the key enzymes responsible for the methanol oxidation of the cells, in that the cells contained no c-type cytochrome and the methanol oxidizing activity from the partially purified alcohol dehydrogenase was too low, respectively. In substrate switching experiments, we found that only a catalase-peroxidase among the three types of catalase found in glucose-grown cells was highly expressed, in the methanol-grown cells and that its activity was relatively high during the exponential growth phase in Mycobacterium sp. JCl. Therefore, we propose that catalase-peroxidase is an essential enzyme responsible for the methanol metabolism directly Of indirectly in Mycobacterium sp. JCl.

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Characterization of PVA Degrading Enzymes from Microbacterium barkeri KCCM 10507 and Paenibacillus amylolyticus KCCM 10508 (Microbacterium barkeri KCCM 10507 및 Paenibacillus amylolyticus KCCM 10508에서 분비되는 PVA 분해 효소의 특성 연구)

  • Choi Kwang-Keun;Kim Sang-Yong;Lyoo Won-Seok;Lee Jin-Won
    • KSBB Journal
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    • v.21 no.1 s.96
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    • pp.54-58
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    • 2006
  • The purpose of this study is to search the characteristics of PVA degrading enzymes which were obtained from Microbacterium barkeri KCCM 10507 and Paenibacillus amylolyticus KCCM 10508, respectively. As a result of the PVA degrading test using crude enzymes, the activity of SAO (secondary alcohol oxidase) was maximized after 2 or 3 days from start of the test, while the activity of BDH (${\beta}$-diketone hydrolase) was gradually increased during the test. Activities of them were maintained in the presence of PVA, but as PVA was gradually degraded, their activity was decreased. PVA was inoculated again into the media, their activity was revealed. This result indicated that above two different enzymes were closely connected with PVA degradation and PVA was degraded by activity of SAO and BDH. Maximum activity of them was 1.5-1.8 unit for SAO and 1.5-2.0 unit for BDH under $35^{\circ}C$ and pH 7.8-8.8, respectively.

The Study of Enzymes Produced by Streptomyces halstedii ssp. scabies SA1-27 and Streptomyces violaceusinger C1-6 Which Have Good Lignolytic Activity (리그닌의 분해가 우수한 Streptomyces halstedii ssp. scabies SA1-27과 Streptomyces violaceusinger C1-6에서 생성되는 효소들에 관한 연구)

  • Kim, Tai-Jeon
    • Korean Journal of Clinical Laboratory Science
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    • v.38 no.2
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    • pp.87-93
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    • 2006
  • This study was done to know a kind and change (transition) of enzymes produceed by Streptomyces halstedii ssp. scabies SA1-27 and Streptomyces violaceusinger C1-6 which showed good lignolytic activity and a good decolorization ratio of remazol brilliant blue R(RBBR) dye. These strains were isolated from soil and identified by the author. The basal medium containg 0.2% glucose was used to measure enzyme activity, Lignin peroxidase 1 (Lip 1) was measured by the methods of Choi, and Bourbonnais and Paice. Lignin peroxidase 2 (Lip 2) was measured by the methods of Ishida et al and Ramachandra et al using 2.4-dichlorophenol(2.4 DCP), manganese peroxidase(Mnp), veratryl alcohol oxidase (VAO), and laccase. They were measured by each of the methods of Choi and Paszczynski et al, and Bourbonnais and Paice, and De Jong et al. In the results, the kind of enzymes produced by Streptomyces halstedii ssp. scabies SA1-27 were Lip 1, Lip 2, VAO, and laccase, and their activities indicated the highest value as each 4.95 nmol/mg protein, $8.45({\times}100^{-3})unit$, 10.25 nmol/mg protein, 9.20 nmol/mg protein on the sixth day of the culture and decreased gradually over time. The kind of enzymes produced by Streptomyces violaceusinger C1-6 were Lip 1, Lip 2, Mnp, VAO, and laccase, and their activities indicated the highest value as each 4.90 nmol/mg protein, $13.85({\times}100^{-3})unit$, 3.10 nmol/mg protein, 11.30 nmol/mg protein, 4.45 nmol/mg protein on the sixth day of the culture and decreased gradually over time. Consequently, the author knew the fact that there were few differences in the kind and quantity of enzymes produced by the two Streptomyces strains, but all enzyme activities indicated the highest value on the sixth day of the culture and decreased gradually over time.

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Protective Effects of Akebia quinata Fruit Extract on Acute Alcohol-induced Hepatotoxicity in Mice (급성 알코올 간독성을 유발한 생쥐에 있어서 으름 열매 추출물의 간 기능 보호효과)

  • Lee, Sang Hoon;Song, Young Sun;Lee, Seo Yeon;Kim, So Young;Ko, Kwang Suk
    • Korean Journal of Food Science and Technology
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    • v.46 no.5
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    • pp.622-629
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    • 2014
  • We studied the effects of Akebia quinata fruit extract (AQ) on acute alcohol-induced hepatotoxicity in mice. AQ (30-1,000 mg/kg body weight (BW) per day) was orally administered to the study group, once daily for 1 week. On the last day of AQ treatment, ethanol (6 mg/kg BW) was orally administered to induce acute liver injury. The AQ-treated group showed significantly lower levels of alanine aminotransferase and aspartate aminotransferase, compared to the only ethanol-treated group (ETG). The glutathione level in the AQ-treated group elevated up to 20.6%, compared to that observed in the ETG. The mRNA expression of glutathione synthetic enzymes was also higher in the AQ-treated group, compared to the ETG. The AQ-treated group also exhibited lower levels of expression of NADPH oxidase 4 and tumor necrosis factor alpha mRNA. Thus, these results show that AQ treatment can be a potential method to reduce oxidative stress and inflammation in ethanol-treated mouse liver and also that AQ can be a useful therapeutic agent for acute alcohol-induced hepatotoxicity.

Effects of Pueraria thunbergiana Bentham Water Extracts on Hepatic Alcohol Metabolic Enzyme System In Rats (칡 열수추출물이 흰쥐의 알콜올 대사효소계에 미치는 영향)

  • 김명주;이정수;하오명;장주연;조수열
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.31 no.1
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    • pp.92-97
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    • 2002
  • The effects of Pueraria flos (PF) and Pueraria radix (PR) water extract on the hepatic alcohol metabolic enzyme activities were examined in rats that were orally administered ethanol (25% v/v, 5g/kg body weight/day) for 5 weeks. The PF and PR water extract were supplemented in a diet, based on 1.2 g or 2.4 g of raw PF or PR/kg body weight/body. Alcohol administration without the PF or PR supplementation significantly decreased net weight gain, feed intake and feed efficiency ratio. However. both dose of the PF of PR supplementation resulted in significant enhancement of growth and suppression of increased relative weight of liver, brain and heart by alcohol administration. Activities of hepatic alcohol dehydrogenase and microsomal ethanol oxidizing system were higher in the alcohol treated group than in the normal group, while aldehyde dehydrogenase activity was significantly lowered in the alcohol treated group. The hepatic metabolic enzyme activities altered by alcohol administration were normalized by both doses of PF or PR supplement. Hepatic monoamine oxidase activity and hydrogen peroxide, which were significantly higher in the alcohol treated group than in the normal group, were also decreased by the supplementation with either PF or PR. These results indicate that low-or high-supplementation of either water extract PF or PR may alleviate ethanol-induced hepatotoxicity by altering alcohol metabolic enzyme activities.

The Inhibitory Effects of Pogostemon cablin Bentham Extract on Melanogenesis (광곽향 추출물의 멜라닌 생성 저해 효과)

  • Bae, Seong-Yun;Lee, Eung-Ji;Son, Rak-Ho;Lee, Yong-Hwa
    • Journal of the Society of Cosmetic Scientists of Korea
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    • v.35 no.1
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    • pp.33-39
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    • 2009
  • To develop a new natural whitening agent for cosmetics, we investigated the inhibitory effects of Pogostemon cablin Bentham extracts (PCE) and its active component on melanogenesis. PCE showed ROS scavenging activities in 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and xanthine/xanthine oxidase system with the $IC_{50}$ values of $24.2{\pm}2.85{\mu}g/mL$ and $IC_{50}=118{\pm}0.43{\mu}g/mL$, respectively. PCE reduced melanin contents of B16 melanoma cells in a dose-dependant manner and decreased to about 23 % at a concentration of $20{\mu}g/mL$ without cell cytotoxicity (below $100{\mu}g/mL$). And the PCE reduced intracellular tyrosinase activity about 18 % at concentration of $50{\mu}g/mL$. We purified one active compound from PCE and identified its structure. It was identified as patchouli alcohol, sesquiterpene family, by 1H-NMR, $13_C$-NMR, and Mass analysis. Patchouli alcohol also inhibited ROS scavenging activities in DPPH radical and xanthine/xanthine oxidase system with the $IC_{50}$ values of $3.14{\pm}0.12{\mu}g/mL$ and $49{\pm}3.24{\mu}g/mL$, respectively. Patchouli alcohol inhibited melanin synthesis in a dose dependent manner ($IC_{50}=3.9{\mu}g/mL$). And the patchouli alcohol reduced intracellular tyrosinase activity about 40 % at concentration of $10{\mu}g/mL$. Patchouli alcohol inhibited tyrosinase and TRP-2 expression at protein level. These results suggest that PCE and patchouli alcohol reduced melanin formation by the inhibited of tyrosinase activity and expression in B16 melanoma cells. Therefore, we suggest that PCE could be used as a useful whitening agent.

Glucose Sensing Properties of Electrospinning-Synthesized ZnO Nanofibers (전기방사로 합성된 산화아연 나노섬유의 Glucose 감응특성)

  • Choi, Jong-Myoung;Byun, Joon-Hyuk;Kim, Sang Sub
    • Korean Journal of Materials Research
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    • v.25 no.12
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    • pp.655-658
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    • 2015
  • The development of glucose biosensors has been attracting much attention because of their importance in monitoring glucose in the human body; such sensors are used to diagnose diabetes and related human diseases. Thanks to the high selectivity, sensitivity to glucose detection, and relatively low-cost fabrication of enzyme-immobilized electrochemical glucose sensors, these devices are recognized as one of the most intensively investigated glucose sensor types. In this work, ZnO nanofibers were synthesized using an electrospinning method with polyvinyl alcohol zinc acetate as precursor material. Using the synthesized ZnO nanofibers, we fabricated glucose biosensors in which glucose oxidase was immobilized on the ZnO nanofibers. The sensors were used to detect a wide range of glucose from 10 to 700 M with a sensitivity of $10.01nA/cm^2-{\mu}M$, indicating that the ZnO nanofiber-based glucose sensor can be used for the detection of glucose in the human body. The control of nanograins in terms of the size and crystalline quality of the individual nanofibers is required for improving the glucose-sensing abilities of the nanofibers.

Planar microchip-based lactate biosensor (평면 소자형 락테이트 바이오센서)

  • Ha, Jeonghan;Huh, Hwang;Kang, Tae Young;Lee, Yong Seok;Yoon, Soon Ho;Shin, Jungwon;Nam, Hakhyun;Cha, Geun Sig
    • Analytical Science and Technology
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    • v.19 no.6
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    • pp.482-489
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    • 2006
  • Two electrode-based lactate biosensor was prepared by immobilizing lactate oxidase (LOD) obtained from pediococcus species in a poly(vinyl alcohol). Hydrogen peroxide ($H_2O_2$) produced by the reaction of lactate and LOD was detected on the Pt-black that was electrochemically deposited on the Au electrode. Sensors fabricated with Pt-black deposited Au electrode provided a high current of $H_2O_2$ oxidation at a substantially lowered applied potential (+300 mV vs. Ag/AgCl), resulting in reduced interferences from easily oxidizable species such as ascorbic acid, acetaminophen, and uric acid. An outer membrane is formulated by adjusting water uptake of hydrophilic polyurethane (HPU). The sensor performance was evaluated in vitro with both flow-through arrangement and static mode. The sensor showed a linear range from 0.1 mM to about 9.0 mM in 0.05 M phosphate buffer (pH 7.6) containing 0.05 M NaCl. Storing the sensors prepared in this work at $4^{\circ}C$ buffer solution while not in use, they provided same electrochemical performance for more than 25 days.

Preventive Effects of Lycopene-Enriched Tomato Wine against Oxidative Stress in High Fat Diet-Fed Rats

  • Kim, A-Young;Jeon, Seon-Min;Jeong, Yong-Jin;Park, Yong-Bok;Jung, Un-Ju;Choi, Myung-Sook
    • Preventive Nutrition and Food Science
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    • v.16 no.2
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    • pp.95-103
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    • 2011
  • This study was performed to investigate the antioxidant mechanism of tomato wine with varying lycopene content in rats fed a high fat diet (HFD). Male Sprague-Dawley rats were randomly divided into five groups (n=10 per group) and fed an HFD (35% of total energy from fat) plus ethanol (7.2% of total energy from alcohol), tomato wine with varying lycopene content (0.425 mg%, 1.140 mg% or 2.045 mg% lycopene) or an isocaloric control diet for 6 weeks. Mice fed HFD plus ethanol significantly increased erythrocyte hydrogen peroxide and thiobarbituric acid reactive substances (TBARS) levels with increases in activities of erythrocyte antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px) and glutathione reductase (GR) compared to pair-fed rats. Supplementation of tomato wine with varying lycopene content decreased ethanol-mediated increases of erythrocyte lipid peroxidation and antioxidant enzyme activities in HFD-fed rats, and tomato wine with higher lycopene appeared to be more effective. Tomato wine also dose-dependently lowered TBARS levels with decreased pro-oxidant enzyme, xanthine oxidase (XOD) activity in plasma of HFD-fed rats. In contrast to erythrocytes, the inhibitory effects of tomato wine on hepatic lipid peroxidation were linked to increased hepatic antioxidant enzymes (SOD and CAT) and alcohol metabolizing enzyme (alcohol dehydrogenase and aldehyde dehydrogenase) activities. There were no significant differences in hepatic XOD and cytochrome P450-2E1 activities among the groups. Together, our data suggest that tomato wine fortified with lycopene has the potential to protect against ethanol-induced oxidative stress via regulation of antioxidant or pro-oxidant enzymes and alcohol metabolizing enzyme activities in plasma, erythrocyte and liver.

Immunological Study of Induction to Salivary Glands the Cytochrome P450(IIE1) by Stress in Rat (백서 타액선의 스트레스 유도 Cytochrome P450 IIE1(CYPIIE1)에 관한 면역학적 연구)

  • Jin-Pyo Lee;Jung-Pyo Hong
    • Journal of Oral Medicine and Pain
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    • v.21 no.2
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    • pp.331-349
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    • 1996
  • Cytochrome P45O is an oxidase involved in oxidation of alcohol and is known to be an activator of carcinogen. The present study was performed to study the effect of alcohol and cold stress on the expression of Cytochrome P450 IIEl (CYPIIE1) In the liver and salivary glands in rats by an immunoblot analysis. Sixteen rats were divided into 4 groups; 1)rats belonging to group I were allowed to take 15%(v/v) ethyl alcohol as a drink ad libitum: 2)rats of group II were bathed in cold water for 30 sec twice a day (during the one-week experiment); 3)rats comprising group III were received alcohol and cold stress as described above; 4)rats of group IV were selected as a control. The rat were sacrificed at the end of the one-week experiment. The livers and parotid and submandibular salivary glands were removed and stored at -2$0^{\circ}C$ until use. The stored organs were homogenized for 10 sec and the supernatants were obtained by centrifugation. The proteins of the supernatants were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and subjected to Western blotting. The blotted membranes were incubated with polyclonal antibodies to CYPIIEI . The obtained results were as follows : 1. The expression of CYPIIEl was apparently negative in the liver and salivary glands of group IV, wheras its expression was marked in the experiment groups I, II. and III. 2. No difference in the expression of CYPIIEl in the liver and salivary glands was observed between the experiment groups I, II, and III. 3. Among the experiment groups, the expression of CYPIIE1 in the liver was much greater than in the salivary glands. The expression of CYPIIE1 in the submandibular gland was weakly positive but was greater than in the carotid gland.

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