• Title/Summary/Keyword: 산화환원효소

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Fabrication and Characterization of Lactate Oxidase-catalase-mitochondria Electrode (젖산 산화효소-카탈라아제-미토콘드리아 전극 제작 및 특성 분석)

  • Ke Shi;Keerthi Booshan Manikandan;Young-Bong Choi;Chang-Joon Kim
    • Korean Chemical Engineering Research
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    • v.62 no.3
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    • pp.238-245
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    • 2024
  • The lactate electrode can be utilized either as an electrode for lactate sensor to monitor the patient's health status, stress level, and athlete's fatigue in real time or lactate fuel cell. In this study, we fabricated a high-performance electrode composed of lactate oxidase, catalase, and mitochondria, and investigated the surface analysis and electrochemical properties of this electrode. Carbon paper modified with single-walled carbon nanotubes (CP-SWCNT) had significantly improved electrical conductivity compared to before modification. The electrode to which lactate oxidase, catalase, and mitochondria were attached (CP-SWCNT-LOx-Cat-Mito) produced a higher current than the electrode to which lactate oxidase and catalase were attached. The amount of reduction current produced by the bilirubin oxidase (BOD)-attached electrode (CP-SWCNT-BOD) was greatly affected by the presence or absence of oxygen in the electrolyte. The fuel cell composed of CP-SWCNT-LOx-Cat-Mito (anode) and CP-SWCNT-BOD (cathode) produced maximum power (29 ㎼/cm2) at a discharge current density of 133 ㎂/cm2. From this study, we had proved that mitochondria is essential for improving lactate sensor and fuel cell performance.

Effect of Terminalia chebula on Physiological Activity in Mice (가자(Terminalia chebula) 추출물이 마우스의 생리활성에 미치는 영향)

  • 박종옥;이승은
    • Journal of Life Science
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    • v.14 no.1
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    • pp.148-153
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    • 2004
  • In this study, we investigated the effect of water, extract of Terminalia Chebula (TC) on physiological activity in mice. TC water extract showed hemagglutination against several different types of red blood cells. $LD_{50}$ of TC extract was 390 mg/kg (po). Treatment of TC water extract orally administered 200, 300 mg/kg daily for one week. Hepatic cytosolic enzymes, xanthine oxidase and aldehyde oxidase activities were significantly increased comparison with normal group. Treatment of TC water extract increased hepatic malondialdehyde (MDA) formation, and reduced glutathione content. We also found that the decreased activities of glutathione S-transferase and glutathione reductase but was not affected activities of $\gamma$-glutamylcysteine synthetase after treatment of TC water extract. These results suggested that increase of the hepatic lipid peroxide is caused by glutathione reduction.

Rapid Detection Methods for Biogenic Amines in Foods (식품 내 바이오제닉아민 신속검출기술 개발 동향)

  • Lee, Jae-Ick;Kim, Young-Wan
    • Korean Journal of Food Science and Technology
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    • v.44 no.2
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    • pp.141-147
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    • 2012
  • Biogenic amines have been used as chemical indicators to estimate bacterial spoilage of foods, particularly fish and fish products, cheese, and fermented foods. So far many chromatography methods have been developed to detect biogenic amines in foods. Although these instrumental analyses exhibit good sensitivity, they cannot be used as rapid detection methods due to the chemical treatment of the samples and the time-consuming process involved. For the rapid and simple detection of biogenic amines, enzyme linked immunosorbent assay kits are commercially available. In addition, analytical systems with enzyme-based amperometric biosensor detection have been increasingly developed. The biosensors used to detect the biogenic amines are based on the action of either amine oxidases or amine dehydrogenases that catalyzes the oxidative deamination of biogenic amines to the corresponding aldehydes and ammonia. This review mainly focused on the principle, development, and applications of the detection methods for rapid detection of biogenic amines in foods.

Purification and characterization of TPx from archeabacteria, Halococcus agglomeratus (고염 원시박테리아(Halococcus agglomeratus)에 존재하는 TPx 분리 및 생화학적 특성연구)

  • Choi, Yong-Soo;Cha, Mee-Kyung;Kim, Il-Han
    • The Journal of Natural Sciences
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    • v.14 no.2
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    • pp.67-82
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    • 2004
  • A thiol-specific antioxidant protein (TSA or TPx) was purified from Halophilic archeabacteria Halococcus agglomeratus, by DEAE-Cellulose, Phnyl, sepharose, Sephadex G-75, Sephacryl S-100, Sephacryl S-200, and Q-Wepharose FF. This protein exhibited the preventeive effect against the inactivation of glutamine synthehase (GS) activity was support by a thiol-reducing equicalent such as dithiothreitol. TPx activity was maximal at NaCl concentration above 500mM. The molecular mass of the protein was determinated to be 22-kDa by SDS-PAGE. The TPx purified from Halococcus agglomeratus seems to be similar to other TPx family, except for the salt requirement for the maximal antioxidant activity.

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Effect of Teminalia chebula Extract on Liver in Rat (가자(Terminalia chebula) 추출물이 흰쥐의 간장 활성에 미치는 영향)

  • 박종옥;이인섭;최종원
    • Journal of Life Science
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    • v.14 no.1
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    • pp.141-147
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    • 2004
  • In this study, we investigated the effect of Teminalia Chebula (TC) water extract on liver in Rat. Treatment of TC water extract was orally administered 200, 300 mg/kg daily for one week and two weeks. The clinical parameters of serum, values of AST, ALT showed significantly higher than in normal group. Xanthine oxidase and aldehyde oxidase activities were significantly increased comparison with normal group. Microsomal enzymes, aminopyrine N-demethylase and aniline hydroxylase were not affected. Water extract of TC also increased hepatic rnalondialdehyde formation and reduced glutathione content. We also found that water extract of TC decreased activities of glutathione S-transferase and glutathione reductase but was not affected activities of $\gamma$-glutamylcysteine synthetase Thus, it seems that the water extract of TC induced decrease of oxygen free radical scavenger, glutathione content by inhibition of glutathione reductase which may reform oxidized glutathione to reduced glutathione.

Physicochemical Property and Antioxidative Activity of Hot-Water Extracts from Enzyme Hydrolysate of Astragalus membranaceus (황기 효소분해물 열수추출액의 이화학적 특성 및 항산화 활성)

  • Kwon, Sang-Chul;Choi, Goo-Hee;Hwang, Jong-Hyun;Lee, Kyung-Haeng
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.3
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    • pp.406-413
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    • 2010
  • To enhance the yield and bioactivity of hot-water extract from herbal medicine, Astragalus membranaceus was hydrolyzed with carbohydrases, such as ClariSEB and Fungamyl. After hot-water extracts were prepared from each hydrolysate (HW-C/F), physicochemical property, antioxidant activity and sensory property were evaluated. The solid content ($^{\circ}Brix$) of HW-C/F was higher than hot-water extract from A. membranaceus no treated enzyme (control). Although pH of HW-C/F was lower than that of the control, the acidity was higher. Lightness of Hunter's color values was increased in HW-C/F whereas redness and yellowness were decreased. The contents of reducing sugar, flavonoid and polyphenol of HW-C/F were higher than the control but the content of ascorbic acid was not different from control. The inhibitory activity of HW-C/F against lipid peroxidation was slightly higher than control, but DPPH radical scavenging, ABTS reducing, metal chelating activities were significantly increased by HW-C/F. The sensory evaluation also revealed that the sensory panelists preferred HW-C/F to that of control. Therefore, hydrolysis by carbohydrases for preparation of hot-water extract from A. membranaceus is one of the good methods to improve antioxidative activity and sensory property of hot-water extract.

Age-Dependent Progesterone Metabolism in the Rat Brain (쥐 뇌의 progesterone대사에 미치는 연령의 효과)

  • Han, Beom-Ku;Park, In-Ho;Jo, Do-Hyun
    • Applied Biological Chemistry
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    • v.38 no.1
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    • pp.37-41
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    • 1995
  • The effect of age on the metabolism of progesterone was studied in the rat brain. Metabolic activity was more active in minced tissues than total homogenates. The activity of progesterone $5{\alpha}-reductase(s)$ was increased during postnatal periods(between 5 and 14 days after birth) and thereafter steadily decreased up to the one-fourth level of the fetus. When $5{\alpha}-dihydroprogesterone$ was incubated with brain tissues of various ages, the change in the activity of $3{\alpha}-hydroxysteroid$ oxidoreductase$(3{\alpha}-HSOR)$ was similar to that of $5{\alpha}-reductase(s)$. These results suggest that the reduced formation of total $5{\alpha}-reduced$metabolites was due to the decreased activities of $5{\alpha}-reductase(s)$ and $3{\alpha}-HSOR$. However the level of $3{\beta}-HSOR$ remained constant regardless of the age.

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The Effects of Pulsed Electromagnetic Fields on Blood components, Antioxidant enzymes and Reactive Oxygen in Hyperlipidemic Rats (맥동전자장이 고지혈증 흰쥐의 혈액 성분, 항산화 효소 및 활성 산소에 미치는 영향)

  • Bang, Hyun-Soo;Jeong, In-Ho;Lee, Sang-Deok
    • Journal of Digital Convergence
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    • v.12 no.7
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    • pp.349-356
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    • 2014
  • The present study was aimed to investigate the effects of the application of pulsed electromagnetic fields on the blood components associated hyperlipidemia, antioxidant enzymes and reactive oxygen. The subjects were divided into three groups: General Diet, High fat Diet, High fat diet and pulsed electromagnetic fields. Pulsed electromagnetic field was applied with pulsed electromagnetic energy therapy equipment. The Glucose, free fatty acids, triglycerides, cholesterol and insulin was used to measure hyperlipidemia-related blood components, and the GSH, GRD, XO and MDA was used to measure antioxidant enzymes and reactive oxygen. The applied pulsed electromagnetic field has improved the concentrations of blood components and increasing GSH and GRD, that were decreased due to a high-fat diet and by reducing the increased MDA and XO to a level of general diet group. Therefore, the applied pulsed electromagnetic field can be the effective treatment for changes in the blood composition of hyperlipidemic rats, enhancement of antioxidative activity and the inhibition of reactive oxygen.

Characterization of Alcohol Dehydrogenase Encoded by Zymomonas mobilis Gene Cloned in Escherichia coli (Escherichia coli 형질전환체가 생산하는 Zymomonas mobilis 알콜 탈수소 효소의 분석)

  • 신병식;윤기홍;박무영
    • Microbiology and Biotechnology Letters
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    • v.18 no.3
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    • pp.268-272
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    • 1990
  • The structural gene (zadhII) encoding an alcohol dehydrogenase II from Zyrnornonas mobilis was cloned into Escherichia coli in our laboratory (Yoon et al., 1989. Kor. J. Microbiol. Biotechnol.). From E. coli (pADS93) carrying the zadhII gene, the Z mobilis alcochol dehydrogenase II (ZADH-II) was purified by sonication, $(NH_4)_2SO_4$, fractionation, and chromatography. The ZADH-I1 enzyme produced by Z. mobilis cell was also purified to compare to the enzyme produced by E. coli (pADS93). The purified enzyme from cell extract of E. coli (pADS93) was identified to be a tetramer being composed of four identical subunits having molecular weight of 40, 000 dalton like that of Z. mobilis. The pH optimum for the reaction oxidizing ethanol to acetaldehyde was 10.0 while the optimum for the reverse reaction was 7.5-8.5. The apparent $K_m$ values for ethanol and NAD + were $1.2 \times 10^{-1}M$and $5.1\times 10^{-5}M$, respectively. In addition, it was found that the $K_m$ value for acetaldehyde was very lower than that for ethanol.

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Molecular Cloning and Gene Expression of Sinorhizobium meliloti Mannitol Dehydrogenase in Escherichia coli, and Its Enzymatic Characterization (Sinorhizobium meliloti 유래 Mannitol Dehydrogenase 유전자의 클로닝 및 대장균 내 발현과 효소특성 규명)

  • Jang, Myoung-Uoon;Park, Jung-Mi;Kim, Min-Jeong;Lee, So-Won;Kang, Jung-Hyun;Kim, Tae-Jip
    • Microbiology and Biotechnology Letters
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    • v.41 no.2
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    • pp.153-159
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    • 2013
  • A mannitol dehydrogenase (MDH; EC 1.1.1.67) gene was cloned from the Sinorhizobium meliloti 1021 (KCTC 2353) genome and expressed in Escherichia coli. It was seen to have an open reading frame consisting of 1,485 bp encoding 494 amino acids (about 54 kDa), which shares approximately 35-55% of amino acid sequence identity with some known long-chain dehydrogenase/ reductase family enzymes. The recombinant S. meliloti MDH (SmMDH) showed the highest activity at $40^{\circ}C$, and pH 7.0 (D-fructose reduction) and pH 9.0 (D-mannitol oxidation), respectively. SmMDH could catalyze the oxidative/reductive reactions between D-mannitol and D-fructose in the presence of $NAD^+/NADH$ as a coenzyme, but not with NADP+/NADPH. These results indicate that SmMDH is a typical $NAD^+/NADH$-dependent mannitol dehydrogenase.