• Title/Summary/Keyword: Ammonium-exchange

Search Result 371, Processing Time 0.029 seconds

Relationship between Land-Use Change and Soil Carbon and Nitrogen (토지(土地) 이용(利用) 형태(形態)의 변화(變化)와 토양(土壤) 내(內) 탄소(炭素)와 질소(窒素의 관계(關係))

  • Son, Yowhan;Lee, Sook Hee
    • Journal of Korean Society of Forest Science
    • /
    • v.90 no.3
    • /
    • pp.242-248
    • /
    • 2001
  • Changes in land-use can affect soil organic matter content and fertility. We compared total soil carbon and nitrogen concentrations, soil respiration, and nitrogen availability under three land-use types in central Korea; conversion of old rice field to natural willow-maple (Salix-Acer) forest, conversion of old field to artificial Korean pine (Pines koraiensis) forest, and indigenous oak (Quercus spp.) forest. After 20 years of fallow the area of rice field conversion to forest had higher soil carbon and nitrogen concentrations in the soil depth of 0-10cm and 10-20cm than the areas of field conversion to Korean pine forest and indigenous forest. In general, soil carbon and nitrogen concentrations decreased with soil depth. Organic matter accumulation as a balance of input and decomposition seemed to be higher in the soil of previous rice field, and carbon and nitrogen accumulation was largely confined to the topsoil. Soil respiration rates were greatest at the area of rice field conversion to forest, and appeared to be related to soil carbon and soil moisture. Soil nitrogen availability measured by the ion exchange resin bag method differed significantly among land-use types; soil inorganic nitrogen ($NH_4{^+}+NO_3{^-}$) and ammonium availability were highest in the soil under indigenous oak forest followed by conversion of old field to artificial Korean pine forest and conversion of old field to natural willow-maple forest.

  • PDF

Purification and Characterization of a Fibrinolytic Enzyme Produced by Bacillus amyloliquefaciens HC188 (Bacillus amyloliquefaciens HC188이 생산하는 혈전분해 효소의 정제 및 특성)

  • Shin, So Hee;Hong, Sung Wook;Chung, Kun Sub
    • Microbiology and Biotechnology Letters
    • /
    • v.41 no.1
    • /
    • pp.33-43
    • /
    • 2013
  • A bacterium producing a fibrinolytic enzyme was isolated from Cheonggukjang. The bacterium was identified as a strain of Bacillus amyloliquefaciens by 16S rDNA analysis and designated as B. amyloliquefaciens HC188. The optimum culture medium appeared to be one containing 0.5% (w/v) maltose and 0.5% (w/v) soytone. Bacterial growth in the optimal medium at $37^{\circ}C$ reached the stationary phase after 27 h of incubation and the fibrinolytic enzyme showed optimum activity at 24 h. The enzyme was purified by 20-80% ammonium sulfate precipitation, CM Sepharose fast flow ion exchange chromatography, and Sephacryl S-200HR column chromatography. Its specific activity was 38359.3 units/mg protein and the yield was 5.5% of the total activity of the crude extracts. The molecular weight was 24.7 kDa and the amino acids of the N-terminal sequence were AQSVPYGVSQIKAPA. The fibrinolytic enzyme activity had an optimum temperature of $40^{\circ}C$ and an optimum pH of 8.0, and the enzyme was stable in the ranges $20-40^{\circ}C$ and pH 6.0-8.0. Enzyme activity was increased by $Ca^{2+}$ and $Co^{2+}$ but inhibited by $Cu^{2+}$, EDTA, and PMSF. It is suggested that the purified enzyme is a metallo-serine protease.

Cytokine Expressions with Lectins from Allomyrina dichotoma and Bombyx mori (장수풍뎅이(Allomyrina dichotoma)와 누에(Bombyx mori) 렉틴의 사이토카인 생성 양상 비교)

  • Kim, Se-Jin;Chung, See-Ryun;Jeune, Kyung-Hee
    • Korean Journal of Pharmacognosy
    • /
    • v.36 no.2 s.141
    • /
    • pp.129-135
    • /
    • 2005
  • Lectins from Allomyrina dichotoma (ADL) and Bombyx mori (BML) were partially purified by physiological saline extraction, ammonium sulfate fractionation, anion exchange column chromatography on DEAE Sephadex A-50 and gel filtration column chromatography on Sephadex G-200. An assay for cytokine expression was carried out by using reverse transcription polymerase chain reaction(RT-PCR). mRNA isolated from PBMC(human peripheral blood mononuclear cells) were stimulated with ADL(O.D.=0.2) and BML(O.D.=0.1) for various times(1,4,8,24,48 and 72 h) and various cytokine mRNA assessed by RT-PCR were shown as follows: The patterns of bands for IL-1 mRNA of BML were very similar with those from ADL and these bands were decreased along the increasing reaction times after showing a strong band at 1 h. However mRNA expressions for IL-2, IL-6, $IFN{\gamma}$ and $TNF{\alpha}$ showed different patterns between ADL and BML. With the effect of ADL, the expression of IL-2 and IL-6 mRNA were continuously detected until 72 h with the strongest band of IL-2 mRNA at 24 h. The strong bands of $IFN{\gamma}$ mRNA were observed from 4 to 8 h but the strongest one of $TNF{\alpha}$ was just observed at 1 h. Meanwhile with BML, the bands for IL-2 and $IFN{\gamma}$ were increased along the increasing reaction times until 72 h. The strongest bands were showed from 4 to 8 h with IL-6 and at 8 h with $TNF[\alpha}$. To verify quantitatively ELISA was used for assay of protein secretions of the cytokine gene with IL-2 and $IFN{\gamma}$ expressed markedly different in RT-PCR. The highest cytokine secretion for IL-2 was demonstrated at 48 h. The production of $IFN{\gamma}$ was markedly increased at 24 h and secreted highest at 72 h. These result suggest that ADL and BML, as inducers of cytokines, can elicit detectable cytokine mRNA from PBMC within the first few hours of stimulation and maintain the production of cytokines for a few days by the methods of RT-PCR and ELISA.

Purification and Characterization of Lipase from Acinetobacter sp. B2 Isolated from Oil­contaminated Soil (유류오염지역에서 분리한 Acinetobacter sp. B2로부터의 Lipase 정제 및 특성)

  • Son Seung Hwa;Park Kyeong Ryang
    • Korean Journal of Microbiology
    • /
    • v.40 no.4
    • /
    • pp.320-327
    • /
    • 2004
  • Three hundreds thirty two bacterial colonies which were able to degrade crude oil were isolated from soil sam­ples that were contaminated with oil in Daejeon area. Among them, one bacterial strain was selected for this study based on its higher oil degrading ability, and this selected bacterial strain was identified as Acinetobactor sp. B2 through physiological-biochemical tests and analysis of its 16S rRNA sequence. Acinetobactor sp. B2 was able to utilize various carbohydrates but did not utilize trehalose and mannitol as a sole carbon source. Acinetobactor sp. B2 showed a weak resistance to antibiotics such as kanamycin, streptomycin, tetracycline and spectinomycin, but showed a high resistance up to mg/ml unit to heavy metals such as Ba, Li, Mn, AI, Cr and Pb. The optimal growth temperature of Acinetobactor sp. B2 was $30^{\circ}C.$ The lipase produced by Acinetobactor sp. B2 was purified by ammonium sulfate precipitation, DEAE-Toyopearl 650M ion exchange chromatography and Sephadex gel filtration chromatography. Its molecular mass was about 60 kDa and condition for the optimal activity was observed at $40^{\circ}C$ and pH 10, respectively. The activation energy of lipase for the hydrolysis of p­nitrophenyl palmitate was 2.7 kcal/mol in the temperature range of 4 to $37^{\circ}C,$ and the enzyme was unstable at the temperature higher than $60^{\circ}C.$ The Michaelis constant $(K_m)\;and\;V_{max}$ for p-nitrophenyl palmitate were 21.8 uM and $270.3\;{\mu}M\;min^{-1}mg^{-1},$ respectively. This enzyme was strongly inhibited by 10 mM $Cd^{2+},\;Co^{2+},\;Fe^{2+},\;Hg^{2+},$ EDTA and 2-Mercaptoethalol.

Characterization of a Fibrinolytic Enzyme from Pickled Anchovy (멸치젓갈유래의 혈전용해호소에 대한 특성)

  • Yang Woong-Suk;Lim Hak-Seob;Chung Kyung Tae;Kim Young-Hee;Huh Man Kyu;Choi Byung Tae;Choi Yung Hyun;Jeong Yong Kee
    • Journal of Life Science
    • /
    • v.15 no.3 s.70
    • /
    • pp.434-438
    • /
    • 2005
  • In the previous study, we isolated a myulchikinase (MK), which has fibrinolytic activity and cytotoxicity to the tumor cell line, from myl- chi-jeot-gal. In this study, the effect of NaCl concentration, metallic ions, pH, temperature, and plasminogen on the activity of MK was analysed. The MK activity was maintained at least $80\%$ activity up to $30\%$ NaCl, which indicates that the enzyme may be halotolerant. The optimal pH and temperature were 8 and $40^{\circ}C$, respectively. The fibrinolytic activity of MK was completely inhibited with 0.5 mM $Hg^{2+}$ and inhibited to $50^{\circ}C$ with 1 mM $Cu^{2+}\;and\;Zn^{2+}$. The MK showed strong activity in plasminogen- rich fibrin plate but not in plasminogen-free fibrin plate. The result indicates that the MK may be a plasminogen activator type fibrinolytic enzyme.

Lowering the Bitterness of Enzymatic Hydrolysate Using Aminopeptidase-active Fractions from the Common Squid (Todarodes pacificus) Hepatopancreas (살 오징어(Todarodes pacificus) 간췌장으로부터 aminopeptidase 활성 획분의 쓴맛 개선 효과)

  • Kim, Jin-Soo;Kim, Hye-Suk;Lee, Hyun Ji;Park, Sung Hwan;Kim, Ki Hyun;Kang, Sang In;Heu, Min Soo
    • Korean Journal of Food Science and Technology
    • /
    • v.46 no.6
    • /
    • pp.716-722
    • /
    • 2014
  • Aminopeptidase-active fractions from crude extract of the hepatopancreas of a common squid (Todarodes pacificus) were obtained using acetone (AC; 30-40%) and ammonium sulfate precipitation (AS; 60-70% saturation), anion exchange (AE-II; 0.2 M NaCl) and gel filtration chromatography (GF-I; 30-50 kDa), respectively. The debittering capacity of GF-I fraction based on the aminopeptidase activity (89.2 U/mg), recovery (56.6%) and sensory evaluation (1.0) was better than that of other fractions. Release of amino acids increased as incubation time was increased, and the bitterness of the enzyme reaction mixtures decreased. Incubation with the GF-I fraction for 24 h resulted in the hydrolysis of several peptides, as revealed by reverse-phase HPLC profiles. Peaks 3, 5 and 6 showed the decreased area (%), whereas peaks 1, 2 and 4 showed the increased area. The GF-I fractions were found to be suitable for reducing bitterness in protein hydrolysates by catalyzing the hydrolysis of bitter peptides.

Assessment for Effect of Water Environment by Addition of Improvement Agents on Sediments (저질 개선제의 주입에 의한 수 환경에 미치는 영향 평가)

  • Kim Woo-Hang;Kim Do-Hee
    • Journal of the Korean Society of Marine Environment & Safety
    • /
    • v.10 no.1 s.20
    • /
    • pp.69-73
    • /
    • 2004
  • Control if Sediment is very important in prawn farm due to the eruption of toxic materials such as unionized $H_{2}S,\;NH_{3}\;and\;NO_3$. In this study, column test was conducted with filter media such as activated carbon, zeolite, oyster shell and iron chloride to evaluate the reduction of toxicity from sediment. ammonia-N($NH_3$) was effectively removed by Zeolite and oyster shell. It was indicated that ammonium ion($NH_4^+$) was removed by ion exchange of zeolite. And the ammonia in the column of oyster shell was existed as the form of $NH_4^+$, which is not toxic for prawn because oyster shell was stably kept at $8{\sim}9g$ of pH. Therefore, some of ammonia($NH_4^+$) was removed by oyster shell. Hydrogen sulfide and COD were effectively removed by adsorption of activated carbon and a partial removal of hydrogen sulfide was accomplished by Oyster shell. Phosphorous was removed by activated carbon, oyster shell and iron chloride. In prawn farm, the concentration of ammonia was increased with increase of pH by algae photosynthesis in the column of activated carbon, zeolite and iron chloride, but it was revealed that pH was stably kept in the column of oyster shell.

  • PDF

Electrodeposition of some Alpha-Emitting Nuclides and its Isotope Determination by Alpha Spectrometry (몇가지 알파입자 방출 핵종의 전해석출 및 알파 스펙트럼 측정에 의한 그의 동위원소 정량)

  • Key-Suck Jung;In-Suck Suh
    • Journal of the Korean Chemical Society
    • /
    • v.27 no.4
    • /
    • pp.279-286
    • /
    • 1983
  • An apparatus was made for the electrodeposition of alpha emitting actinide nuclides, $^{207}Bi$ and $^{210}Po$. The electrodeposition was made on a polished stainless steel plate cathode. The anode was made of platinum wire and to stir the solution. With the ammonium chloride as electrolyte initial pH = 4, chloride concentration = 0.6M and solution volume = 15ml, a current of 1.5 ampere(current density = 0.59A/$cm^2$) was flowed for 100 minutes for the quantitative recovery of electrodeposition and on average recovery of 98.3% was obtained within ${\pm}$0.7% uncertainty. Alpha spectrometry of the electrodeposited sample showed alpha peaks from $^{210}Po, ^{234}U$ and $^{239}Pu$ having energy resolution (FWHM) of 18.3, 21.8 and 36.0 keV respectively. The electrodeposition and alpha spectrometry for a natural uranium sample of domestic origin gave $^{238}U : ^{234}U = 1 : 6.1{\times}10^{-5}$ and for a neutron-irradiated uranium sample did $^{238}U : ^{239}Pu : ^{241}Am = 100 : 0.0263 : 5.20{times}10^{-5}$. The result of $^{238}U$ determination in the irradiated sample by electrodeposition-alpha spectrometry was in accord within ${\pm}1.6%$ of relative error with the results of solid fluorimetry and mass spectrometry. For $^{239}Pu$ the result of electrodeposition-alpha spectrometry was in accord within ${\pm}$4.0% of relative error with the results of anion exchange separation and the thenoyltrifluoroacetone(TTA) extraction both followed by alpha spectrometries.

  • PDF

Purification and Assay of Extracellular Autolysin from Moraxella sp. CK-l (Moraxella sp. CK-1의 세포외 Autolysin의 분리 정제 및 활성도 측정)

  • 오영상;이장현;한명수;윤문영
    • Korean Journal of Microbiology
    • /
    • v.39 no.3
    • /
    • pp.148-154
    • /
    • 2003
  • Moraxella sp. CK-l is known to inhibits the growth of Anabaena cylindrica, a cyanobacterium. It has been documented that the ability of this growth inhibition of Anabaena cylindrica was attributed to extracellular autolysin from Moraxella sp. CK-l. However, it remains to be elucidated identification and characterization of autolysin have yet been elucidated. In this study, we tried to purify and identify autolysin secreted from Moraxella sp. CK-l. Cells were grown in a complex liquid medium (BGC-11) and culture supernatants were collected, followed by ammonium sulfate fractionation. Fractions were further separated with anion exchange column, Mono-Q, in FPLC system and analyzed by SDS/PAGE. The fraction containing high autolysin activity showed a single distinct protein peak in anion column and molecular mass of about 17 kDa in SDS/PAGE. Nterminal amino acid sequencing of the protein was analyzed, of which result showed the homology with some proteases, including extracellular serine protease, Dichelobacter nodosus.

Partial Purification and Some Properties of Amylases from Germinating Corn(Zea mays L.) (발아 옥수수 amylases의 정제 및 특성)

  • Lee, Tae-Ho;Jung, Tae-Yung;Park, Mi-yeon
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.19 no.6
    • /
    • pp.625-635
    • /
    • 1990
  • The purpose of this study was focused on investigation of biochemical properties of amylases in germinating corn(Zea mays L.) the amylase(I), (II) and (III) from germinating corn seeds were partially purified by ammonium sulfate precipitation, DEAE-Sephadex A-50 ion exchange column chromatography and Sephadex G-100 gel filtration. The last step was effective for separation of the corn amylases to a homogeneous slate. the purified amylase(I) was identified as a kind of $\alpha$-amylase from the fact that 5% starch solution was hydrolysed into mainly maltose and maltotetrose by it, and amylase(II) and amylase(III) were enzymes producing maltotetrose as main product. The molecular weight and specific activity of the amylase(I), (II) and (III) were determined to be 54,000 and 70.47 unit/mg, 39,000 and 62.98 unit/mg, and 51,000 and 80.39 unit/mg, respectively. It showed a tendency to increase the amylases activities in presence of Ba, Ca, Co and Fe groups, but inhibits in that of Ag, Sn, Hg and Zn groups, and amylase(I), (II) and (III) remained stable at pH 5-6 and 2$0^{\circ}C$ for 40 days in containing of 1 mM CaCl$_2$. The optimum pH and optimum temperatures were pH 6, pH 5 and pH 6 and 35$^{\circ}C$, 55$^{\circ}C$ and 55$^{\circ}C$, respectively. These results suggest that the amylase(I), (II) and (III) were different amylases.

  • PDF