• Title/Summary/Keyword: dehydrogenase

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Relationship between Toxicity of Heavy Metals and Sludge Retention Time in Sequencing Batch Reactor Process (연속회분식반응조 공정에서 슬러지 체류시간과 중금속 독성의 관계)

  • Kim, Keum-Yong;Cho, Young-Cheol;Lee, Sang-Ill
    • Journal of Korean Society of Environmental Engineers
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    • v.29 no.3
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    • pp.283-288
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    • 2007
  • In order to elucidate the relationship between the sludge retention time(SRT) and the toxicity of heavy metals, such as copper (Cu), cadmium(Cd), and zinc(Zn), in sequencing batch reactor(SBR) process, IC50 was estimated with measuring of INT-dehydrogenase activity in variable SRTs. When the concentrations of heavy metals were increased, the activity of INT-dehydrogenase was gradually decreased indicating the heavy metals inhibit bacterial activity. Cu showed higher toxicity than Zn and Cd. $IC_{50}$ of Cu, Cd, and Zn ranged from $0.37\sim1.96$ mg/L, $15.4\sim16.9$ mg/L, and $9.70\sim23.4$ mg/L, respectively. The toxicity of Cu and Zn was reversely proportional to the length of SRT. It is probably caused by the increased concentration of extracellular polymeric substances in longer SRT which absorb heavy metals. Therefore, the operation of SBR with increased SRT is desirable in treatment of industrial wastewater containing heavy metals.

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

  • Kim, Chun-Seong;Song, Gyu-Yeong;Kim, Seong-Jun;Kim, Ho-Sang;Park, Hyeon-Gyun;Lee, Suk-Yeong;Park, Jong-Pil
    • KSBB Journal
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    • v.14 no.5
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    • pp.528-533
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    • 1999
  • Membrane-bound alcohol dehydrogenase(ADH) was purified to homogeneity from the acetic acid producing bacteria, Acetobacter sp. CS5. The enzyme was solubilized and extracted with Trition-X and purified using the DEAE-Sephacel chromatography and Sephacryl S-200 chromatography. The enzyme was purified to 14-fold with a yield of 15%. The molecular weight of the purified enzyme was to be 332 KDa. SDS-PAGE of the enzyme showed three subunits with molecular weights of 79 KDa, 49KDa and 46K Da. It indicated that enzyme consisted of three subunits of the 79 KDa, two subunits of the 49 KDa and. 46 KDa, respectively. The apparent Km value for ethanol was 0.77 mM and the optimum pH and temperature was 4.0-5.0 and 35$^{\circ}C$, respectively.

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Effects of Gamma Irradiation on the Fermentative Microorganisms and Lactate Dehydrogenase Activity in Kimchi at Different Fermentation Stages

  • Yook, Hong-Sun;Kim, Dong-Ho;Song, Hyun-Pa;Lee, Hyun-Ja;Byun, Myung-Woo
    • Preventive Nutrition and Food Science
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    • v.8 no.3
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    • pp.265-269
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    • 2003
  • Gamma irradiation treatment was performed at the early and mid-fermentation stages of Kimchi preparation. Changes in fermentative microorganisms and lactate dehydrogenase activity during the fermentation periods were investigated to determine proper irradiation point for extending the shelf life of Kimchi. Initial levels of acid producing bacteria and yeast in Kimchi were 10$^4$ CFU g$^{-1}$ and 10$^1$ CFU g$^{-1}$ , and reached up to 10$^{9}$ CFU g$^{-1}$ after 15 days and 10$^{7}$ CFU g$^{-1}$ after fermentation for 30 days at 1$0^{\circ}C$, respectively. The radiation resistance of acid producing bacteria in the earlier stage (D$_{10}$ value was 0.87 kGy) was higher than at the midfermentation stage (after 10 days at 1$0^{\circ}C$, D$_{10}$ value was 0.69 kGy). Microbial growth and lactate dehydrogenase activity were inhibited significantly by gamma irradiation at the early fermentation stage of Kimchi and acidification was effectively delayed during the subsequent storage period. Although the growth of fermentative microorganisms was inhibited by gamma irradiation at the mid-fermentation stage of Kimchi, lactate dehydrogenase activity was maintained and acidification continued during the storage period.

Effect of Hepatic Damage on the Toluene Metabolism in Carbon Tetrachloride Pretreated-Rats (흰쥐에 있어서 톨루엔 대사에 미치는 간손상의 영향)

  • Cha, Sang-Eun;Yoon, Chong-Guk;Lee, Sang-Il
    • Toxicological Research
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    • v.14 no.3
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    • pp.321-328
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    • 1998
  • This study was performed to evaluate the effect of liver damage on toluene metabolism in rats pretreated with carbon tetachloride. Liver damage in rats was induced by administration of 0.1ml of carbon tetrachloride per 100g of body wight intraperitoneally every day for four weeks except the last day before sacrifice. One day before sacrifice, toluene was administered to the animals instead of carbon tetrachloride. Rats were sacrificed at the 1st, the 2nd, the 3rd and the 4th week after the first administration of carbon tetachloride. Based on the histopathological findings, liver weight and serum alanine aminotransferase, the $CCl_4$-preteated group was found to have gradual severe liver damage. Especially the degree of liver injury became increasingly severe throughout the whole course of the experiment. The contnts of hippuric acid in urine lower in the all groups pretreated with $CCl_4$than that of the control. The contents of hepatic cytochrome P450(CYP), benzylalcohol dehydrogenase and benzaldehyde dehydrogenase activities were decreased in $CCl_4$-pretreated rats than those of the control. The $CCl_4$treated animals showed the gradual decreased activities of these enzyme as injection times elapsed. Km values of the benzylalcohol dehydrogenase in pooled liver samples from $CCl_4$-pretreated or control groups were similar. On the other hand, Vmax values of the $CCl_4$-pretreated group was lower than of the control. Therefore, it can be concluded that reduction of the toluene metabolism in damaged rat liver induced with $CCl_4$was due to the inhibition of CYP content, bezylalcohol and benzaldehyde dehydrogenase activities which related with toluene metabolic enzyme system.

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The Expression and Functional Analysis of Recombinant Alcohol Dehydrogenase (재조합 alcohol dehydrogenase의 발현 및 기능분석)

  • Kong, Kwang-Hoon;Shim, Eun-Jung;Park, Hee-Joong;Kim, Eun-Ho;Cho, Sung-Hye;Park, Sung-Woo;Kim, Young-Mann
    • Analytical Science and Technology
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    • v.12 no.6
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    • pp.565-570
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    • 1999
  • The alcohol dehydrogenase (ADH) gene from Bacillus stearothermopilus was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pGEX-KG, and expressed it as a fusion protein with glutathione S-transferase (GST) in E. coli. The recombinant ADH was produced by induction with 1 mM isopropyl-${\beta}$-D-thiogalactopyranoside at $37^{\circ}C$ and purified by glutathione affinity chromatography. The recombinant ADH exhibited high substrate specificity for ethanol. The activity of the recombinant ADH proceeded optimally at pH 9.0 and $70^{\circ}C$. The recombinant ADH was highly stable against high temperature. This thermostable alcohol dehydrogenase can be used for the enzymatic determination of alcohol and for the industrial production of alcohol.

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

  • Yoo, Jin-Cheol;Sim, Jung-Bo;Kim, Heung-Keun;Chun, Hong-Sung;Kim, Sung-Jin
    • Korean Journal of Microbiology
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    • v.32 no.1
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    • pp.78-83
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    • 1994
  • Membrane-bound alcohol dehydrogenase(ADH) was purified to homogeneous state fron an acetic acid producing bacteria, Acetobacter sp. HA. The enzyme was purified about 153-fold with an overall yield of 35% from the crude cell extract by solubilization and extraction of the enzyme with Triton X-100 and subsequent fractions by column chromatography. Upon sodium dodecyl sulphate-PAGE, the enzyme showed the presence of three subunits with a molecular mass of 79,000 daltons, 49,000, and 45,000 daltons, respectively. Absorption oxidized aliphatic alcohols with a straight carbon chain except for methanol. Formaldehyde, acetaldehyde and glutaraldehyde were also oxidizable substrates. The apparent $K_m$ for ethanol was 1.38mM. The optimun pH and temperature were 5.0~6.0 and 32${\circ}C$, respectively. $V_2O_5$ and heavy metals such as $ZnCl_2\;and\; NiCl_2$ were inhibitory to the enzyme activity.

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Short-chain Acyl-CoA Dehydrogenase Deficiency in an Asymptomatic Neonate (무증상 신생아에서 진단된 경쇄 acyl-CoA 탈수소효소 결핍증 1례)

  • Lee, Yeonhee;Kim, Jinsup;Huh, Rimm;Cho, Sung Yoon;Jin, Dong-Kyu
    • Journal of The Korean Society of Inherited Metabolic disease
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    • v.15 no.2
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    • pp.93-97
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    • 2015
  • Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is an autosomal recessive hereditary metabolic disorder of mitochondrial fatty acid beta-oxidation. Mutations in the ACADS gene cause short-chain acyl-CoA dehydrogenase deficiency, which is characterized by developmental delay, hypotonia, seizure, and hypoglycemia. Here, we describe one Korean pediatric case of SCAD deficiency, which was diagnosed during newborn screening by tandem mass spectrometry and confirmed by molecular analysis. The level of C4 was typically elevated 5.23 mg/dL (reference range <1.5 mg/dL). This patient had a homozygous mutation [c.1031A>G, p. E344G] in ACADS. Therefore, we present a case of SCAD deficiency in an otherwise healthy neonate and her subsequent development and growth over four years.

Changes of Glucose-6-Phosphate Dehydrogenase on Alloxan-induced Diabetic Rat (Alloxan으로 유발된 당뇨쥐의 간조직 Glucose-6-Phosphate Dehydrogenase 효소의 변화)

  • 박수영;조경혜
    • Biomedical Science Letters
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    • v.3 no.2
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    • pp.169-175
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    • 1997
  • The hypoglycemic and metabolic effects of Commelina communis L. extract were investigated in alloxan-induced diabetic rats. The increased blood glucose level in the diabetic rats was sinificantly lowered with the treatments of the plant protein extract. Administration of the plant extract ellicited the significant increase of glucose-6-phosphate dehydrogenase (G6PD) activity in liver of alloxan-induced rats. Three isozyme patterns(band I, II & III : in order decreasing mobility) of G6PD were found when normal rat liver extract were subjected to electrophoresis on native polyacrylamide gel. On the other hand, G6PD band patterns of alloxan-induced rat liver extract were found band II isozyme missing. By treatment of plant extract in alloxan-induced rats has been showed pattern the recovery of missing band patterns. This indicates that changes of the G6PD isozyme might be related to the cellular process of diabetes.

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Effect of Tillage System and Fertilization Method on Biological Activities in Soil under Soybean Cultivation (경운방법과 시비방법이 콩 재배 토양의 생물학적 활성에 미치는 영향)

  • Oh, Eun-Ji;Park, Ji-Su;Yoo, Jin;Kim, Suk-Jin;Woo, Sun-Hee;Chung, Keun-Yook
    • Korean Journal of Environmental Agriculture
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    • v.36 no.4
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    • pp.223-229
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    • 2017
  • BACKGROUND: Tillage systems and fertilization play an important role in crop growth and soil improvement. This study was conducted to determine the effects of tillage and fertilization on the microbial biomass C and dehydrogenase activity of soils in a field under cultivation of soybean. METHODS AND RESULTS: An experimental plot, located in the temperate climate zone, was composed of two main sectors that were no-tillage (NT) and conventional tillage (CT), and they were subdivided into four plots, respectively, in accordance with types of fertilizers (non fertilizer, chemical fertilizer, hairy vetch, and liquid pig manure). Microbial biomass C and dehydrogenase activity were evaluated from May to July in 2016. The microbial biomass C and dehydrogenase activity of NT soils were significantly higher than those of CT in all fertilizer treatments, and they were further increased in hairy vetch treatment than the other fertilizer treatments in both NT and CT. The dehydrogenase activity was closely related to microbial biomass C. CONCLUSION: It is concluded that application of green manure combined with no-tillage can provide viable management practices for enhancing microbial properties of soil.

Metabolic Pathway of L-Malate in Malo-Alcoholic Fermentation (Malo-Alcohol 발효(醱酵)에 있어서 사과산의 대사경로(代謝経路))

  • Chung, Ki-Taek;Yu, Tae-Shick;Song, Hyung-Ik;Kim, Jae-Kuen;Kim, Chan-Jo
    • Korean Journal of Food Science and Technology
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    • v.16 no.1
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    • pp.90-94
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    • 1984
  • We deduced a possible metabolic pathway of L-malate in a malo-alcoholic yeast, Schizosaccharomyces japonicus var. japonicus St-3. The malic enzyme (EC 1.1.1.40) prepared from the microorganism was about four times as active as that of malate dehydrogenase (EC 1.1.1.37). And Km values of malic enzyme and malate dehydrogenase for malate were found to be 3.125 mM and 4.761 mM, respectively, which referred to the fact that the affinity of malic enzyme for the substrate was greater than that of malate dehydrogenase. We also found that pyruvate was produced with disappearing malate in malo-alcoholic fermentation, and that the addition of $Mn^{2+}$ activated malic enzyme activity. Based on these results obtained we have deduced a main pathway of malate${\rightarrow}$pyruvate${\rightarrow}$acetaldehyde${\rightarrow}$ethanol for the utilization of L-malate by this malo-alcoholic yeast strain.

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