• Title/Summary/Keyword: L-arabinose and L-ribose

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Simulation of SMB [Simulated Moving Bed] Chromatography for Separation of L-ribose and L-arabinose by ASPEN chromatography (L-ribose와 L-arabinose 분리를 위한 Aspen chromatography를 이용한 SMB [Simulated moving bed] 전산모사)

  • Lee, Seon-Hee;Lee, Eun;Kim, In-Ho
    • KSBB Journal
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    • v.23 no.2
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    • pp.135-141
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    • 2008
  • SMB (simulated moving bed) chromatography is a very useful utility for the separation of binary system. We simulated the separation of L-arabinose and L-ribose from the mixture by using lab-scale 4(1-1-1-1)-zone SMB chromatography. Preliminary experiments of PIM (pulse input method) were performed to measure adsorption isotherms of L-ribose and L-arabinose in $NH_2$ HPLC column, and experimental and simulated results from ASPEN chromatography were compared. To find the most suitable separation condition in SMB, we carried out a simulation in $m_2-m_3$ plane base on the triangle theory and calculated operating parameters (flow rate of four zone, switching time and feed concentration and so on) using ASPEN chromatography under the conditions of linear isotherms obtained from PIM.

Determination of Adsorption Isotherms and Separation of L-arabinose and D-ribose in Cation Exchange Chromatography and HPLC (양이온 교환 크로마토그래피와 HPLC에서의 L-arabinose와 D-ribose의 분리 및 등온 흡착곡선 결정)

  • Jeon, Young-Ju;Kim, In-Ho
    • KSBB Journal
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    • v.23 no.1
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    • pp.31-36
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    • 2008
  • The use of L-carbohydrates and their corresponding nucleosides in medicinal application has greatly increased. For example L-ribose has been much in demand as the starting material for curing hepatitis B. High performance liquid chromatography (HPLC) method was studied for the analysis of ribose and arabinose fractions from ion exchange chromatography (IEC). Dowex Monosphere 99 Ca/320 resin was packed in IEC to separate ribose and arabinose under various operating conditions. $NH_{2}$ and sugar HPLC columns were then used to analyze the fractions from the IEC column. Pulse input method (PIM) was also used to measure adsorption isotherms of ribose and arabinose in the Dowex column and HPLC columns. Experimental results and simulations by ASPEN chromatography were compared with fair agreement.

Epimerization of L-Arabinose for Producing L-Ribose (L-리보스 생산을 위한 L-아라비노스의 에피머반응)

  • Jeon, Young Ju;Song, Sung Moon;Lee, Chang Soo;Kim, In Ho
    • Korean Chemical Engineering Research
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    • v.49 no.5
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    • pp.628-632
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    • 2011
  • L-ribose has recently attracted interest as a starting material for antiviral drug. It could be obtained from L-arabinose by epimerization reaction. Epimerization reaction was carried out with molybdenium oxide or molybdic acid catalyst and methanol/water solution. Reaction temperature, methanol percentage, and catalyst kind were selected to find an optimum reaction condition. Ion exhange chromatography was used for separating epimerization reaction mixture, and then HPLC chromatogram of L-ribose fraction obtained to calculate the yield of the reaction. Shodex ion exchange HPLC column(Model SC1011) and Phenomenex Luna $NH_2$ HPLC column were compared to employ a convenient HPLC analysis. It was found that the usage of 20% methanol, $60^{\circ}C$, and 40 g/L molybdic acid gives the best reaction condition with a yield of 21%.

Purification and Characterization of the D-xylulokinase from Candida sp. L-16 (Candida sp. L-16이 생산하는 D-Xylulokinase의 정제 및 특성)

  • 이종수;주길재
    • Food Science and Preservation
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    • v.9 no.4
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    • pp.429-433
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    • 2002
  • The D-xylulokinase from Candida sp. L-16 was purified through a sequence of ammonium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-100 and Sephadex G-200 gel filtration. The specific activity of the purified Dxylulokinase was increased to 23.2 fold and the yield was 11.2%. The enzyme was showed to be a single protein band by SDS-PAGE. The molecular weight of the enzyme was 150,000 dalton, this enzyme was identified to be a dimer with two subunits. The optimum conditions of the enzyme were pH 8.0 and 40$\^{C}$, respectively. The enzyme was relatively stable between pH 7.0 to pH 9.0, but it was unstable over 30$\^{C}$. The enzyme showed substrate specificity on D-xylulose, D-arabinose and D-ribose, Km value and Vmax for D-xylulose were 0.042 mM and 117 units/ml, respectively. The activation energy of the enzyme was 4.75 Kcal/mol. The one was inhibited by metabolic intermediates such as 6-phosphogluconic acid, 2-keto-gluconic acid. The enzyme was activated by EDTA and thiol compounds such as cysteine-HCI, DTT and glutathione.

Studies on the Streptococcus suis isolated from slaughtered pigs (도축돈에서 분리된 Strptococcus suis에 대한 연구)

  • 윤선종;고홍범
    • Korean Journal of Veterinary Service
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    • v.20 no.3
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    • pp.281-288
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    • 1997
  • Streptococcus suis has been identified as a major cause of contagious disease in pigs Ithas been isolated worldwide from pigs suffering from meningitis, bronchopneumonia, polyserositis, polyarthritis and septicemia. Two hundred and fifty-five lung samples of slaughter pigs with gross lung lesions were collected from Jan. to Dec. 1995 in southern Chonnam area. Isolation of S suis were tested by biochemical, serological methods and antimicrobial susceptibility. The results were summerrized as follows ; 1. S suis was Isolated from 30 of 254 pneumonic lungs, 14 Isolates were isolated only, 12 were isolated with p. multocida and 4 were isolated with unidentified Gram positive cocci. 2. In biochemical characteristics studies, all isolates were not grown in 6.5% NaCl medium, and most isolates utilized L-leucine-2-naphtylamide and trehalose, didn't utilize sorbitol, ribose and L-arabinose. 3. In slide agglutination test, 6(20%) Isolates were classified as serotype 2, 4(13.3%) isolates were as serotype l/2, 16, 2 and 2(6.6%) were as serotype 1, 4, 13. 4. S suis isolates showed marked susceptibility to amoxicillin, oxacillin, cephalothin and cepoferazone and high resistance to kanamycin, streptomycin, tetracycline and erythromycin.

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Taxonomic Studies on the Cellulolytic Bacterium Cellulomonas uda CS 1-1 (섬유소 분해균 Cellulomonas uda CS 1-1의 분류학적 연구)

  • Kim, Mi-Seog;Yoon, Min-Ho;Choi, Woo-Young
    • Korean Journal of Agricultural Science
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    • v.34 no.2
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    • pp.99-109
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    • 2007
  • Cellulomanas sp. CS 1-1 was studied for its morphological, physiological and biochemical characteristics, together with DNA homology and fatty acid pattern to elucidate its taxonomical position in the species level. Colony morphology of CS1-1 exhibited circular form, opaque, convex, entire edge and pale yellow. Cells were of rod with the size of $0.3{\sim}0.5{\times}0.8{\sim}1.2{\mu}m$, while coryneforms were formed at the early stage of culture. D-ribose, raffinose, rhamnose, acetate, propionate, L-lactate, D-gluconate, aspartate and proline were not utilized as a sole source of carbon, whereas saccharose, arabinose, and amlyose were utilized. Biochemical characteristics of CS1-1 were Gram positive, catalase positive, oxidase negative, nonmotile, facultative anaerobic, mesophilic and G+C content of 74.7 mol %. The major fatty acid and menaquinone were 12-methyltetradecanoic acid(anteiso-$C_{15:1}$) and MK-$9(H_4)$, respectively. These results were correspondent with the characteristics reported for member of the genus Cellulomonas. The strain CS 1-1 exhibited a high level of DNA homology as 70% with C. uda ATCC491, compared to those of 54~59% with C. fimi ATCC 15724, 46~48% with C. biazotea, C. gelida and C. bibula. Finally, strain CS1-1 could be classified as a novel species belongs to C. uda.

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Formation of D-Glucose Isomerase by Streptomyces sp. (Streptomyces sp.에 의한 포도당 이성화효소의 생성)

  • Rhee, In-Koo;Seu, Jung-Hwn
    • Microbiology and Biotechnology Letters
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    • v.8 no.3
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    • pp.173-180
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    • 1980
  • A source of D-xylose was required for the enhanced production of D-glucose isomerase of Streptomyces sp. strain K-17. D-glucose supported the luxuriant growth of the organism as well as D-xylose, but D-glucose isomerase activity was hardly detected in the D-glucose-grown cells. When the D-glucose-grown cells were incubated aerobically for a few hours in 0.5% xylose solution in 0.05 M phosphate buffer, pH 7.0, it was found that inductive formation of D-glucose isomerase occurred in the cells without multiplication. In the non-growth phase of cells the inductive formation of D-glucose isomerase occurred because a source of nitrogen for the synthesis of enzymes was obtained from turnover of protein accumulated in cells. D-ribose, L-arabinose, D-glucose, D-mannose, citrate, succinate and tartrate could not induce the formation of D-glucose isomerase, but D-xylose could induce. Inductinn of D-glucose isomerase was repressed by D-glucose and its catabolites : glycerol, succinate and citrate. Inductive formation of the enzymes in the non-growth phase was stimulated by $Ba^{2+}$, $Mg^{2+}$ and $Co^{2+}$, and inhibited by C $u^{2+}$, C $d^{2+}$, A $g^{+}$and H $g^{2+}$. The synthesis of enzymes in the induction system composed of 0.5% xylose solution was disrupted by actinomycin D, streptomycin, chloramphenicol, kanamycin, tetracycline, p-chloromercuribenzo ate, arsenate and 2, 4-dinitrophenol, but not disrupted by mitomycin C and penicillin G.icillin G.

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Fermentation Properties of Amylase Activity and Added Rice Yogurt of Enterococcus faecium KHM-11 Isolated from Korean Human Milk (한국인 모유로부터 분리한 Enterococcus faecium KHM-11의 Amylase 활성과 쌀 첨가 요구르트의 특성)

  • Bae, Hyoung-Churl;Lee, Jo-Yoon;Renchinkhand, Gereltuya;Nam, Myoung-Soo
    • Korean Journal of Agricultural Science
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    • v.37 no.3
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    • pp.387-392
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    • 2010
  • This studies were carried out to assess fermentation properties of amylase activity and added rice yogurt of Enterococcus faecium KHM-11 isolated from Korean human milk. The amylase activity of Enterococcus faecium KHM-11 was above 23 units. Characterization of carbohydrate fermentation of Enterococcus faecium KHM-11 has D-ribose, D-lactose, L-arabinose and starch. Titratable acidity and viable count of lactic acid bacteria of 4% rice yogurt was higher compared to the 0%. Therefore we were discussed Enterococcus faecium KHM-11 is suitable microorganism for fermented milk added rice powder. Hydrolysates of sugars of fermented milk with 4% rice powder cultured Enterococcus faecium KHM-11 were analyzed by TLC and HPLC. Hydrolysates of lactose and galactose were revealed and hydrolysates of glucose was not revealed in results of TLC and HPLC.

Effects of Feeding Xylose on the Growth of Broilers and Nutrient Digestibility as well as Absorption of Xylose in the Portal-drained Viscera

  • Peng, Y.L.;Guo, Y.M.;Yuan, J.M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.17 no.8
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    • pp.1123-1130
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    • 2004
  • Two experiments were conducted to examine the effects of dietary inclusion of xylose on growth performance, nutrient digestibility and xylose absorption in the portal-drained viscera of broiler chicks. In Exp. 1, ninety male 14 day-old broilers were used to study the effects of different inclusion levels (0, 5, 10, 20 and 40%) of D-xylose in the semi-purified diets on the growth and nutrient digestibility of broilers. In Exp. 2, One hundred and eight male broilers, fed by precision feeding at 22 day-old, were used to investigate the absorption and transportation of dietary xylose in the portal-drained viscera of broiler. The results of Exp. 1 indicated that the growth of broilers was gradually decreased as the xylose level increased (p<0.01). With the xylose supplementation increased, the moisture in broiler excreta was gradually elevated (p<0.01), AME and the digestibilities of crude protein and ether extract were significantly reduced and the digestibilities of xylose and arabinose were also decreased (p<0.01). The results of Exp. 2 showed that the concentrations of ribose, xylose and galactose in serum were significantly influenced by different dietary levels of xylose (p<0.01), but there's no apparent difference among rhamnose, glucose and arabinose (p>0.05). The xylose concentration in serum was highest in Vena Cava, middle in Portal Vein and lowest in Ulnar Vein within 6 h after precision feeding. And then the xylose concentration in Portal Vein and Ulnar Vein were higher than that of Vena Cava. The concentration of ribose, xylose and galactose in serum were also significantly changed with time prolongation (p<0.01). The concentration of xylose in serum was highest in the 40% xylose treatment, middle in the 20% xylose group and lowest in the control group. The glycogen contents in liver and muscle were linearly decreased as the level of xylose increased (p<0.01). The higher the dietary level of xylose was, the lower digestibility of dietary xylose was (p<0.10). 40% xylose markedly decreased the digestibility of dietary glucose (p<0.01). In conclusion, high levels of xylose in the diets inhibited the growth and nutrient digestibility of broiler. The outputs of xylose from the hydrolyzation of wheat-based diet by xylanase should have no adverse effects on broiler performance.

Characterization of D-Xylose Isomerase from Streptomyces albus (Stleptomyces albus의 D-Xylose Isomerase의 성질에 관하여)

  • 김영호;하영칠
    • Korean Journal of Microbiology
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    • v.16 no.2
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    • pp.47-61
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    • 1978
  • Strptomyces albus T-12 which ahd been isolated and identified in the laboratory, was selected for the studies on the cultural conditions on the production of D-xylose iosmerase and the enzymological characteristics using the partially purified enzyme. The best results in the enzyme production came from D-xylose medium than wheat bran. The divalent metla ions as $Co^{2+},\;Fe^{2+},\;Zn^{2+}\;and\;Cu^{2+}$ retard or inhibit the cell-growth at the early stages of mycelia propagations, and T-12 strain is especially sensitive to $Co^{2+}$. After 60 hours of shaking cultivation at $30^{\circ}C$ and 200 rpm, a maximum enzyme activitz, 0.49 enzyme units, was obtained. Cell-free enzyme obtained from mycelia heat-treated in the prescence of 0.5mM $Co^{2+}$, showed a 2.4-fold increase in specific than the enzyme from untreated mycelia. The specific activity of the purified enzyme through Sephadex G-150 columm showed 180 fold to the crude enzyme. The effective activators of the enzyme appeared to be $Mg^{2+}\;and\;Co^{2+}$ ions, and it exhibited the maximal enzyme activity showed at pH 7.0 and at tempersture around $80^{\circ}C$ when $Mg^{2+}\;and\;Co^{2+}$ ions were added. The enzyme isomerized D-glucose, D-xylose, D-ribose, L-arabinose, D-mannose, and L-rhamnose in the present of $Mg^{2+}\;and\;Co^{2+}$ ions as an activatiors. $Mg^{2+}\;and\;Co^{2+}$ ions were non-competitively bound at different allosterix sites of enzyme molecule. $Mg^{2+}(5mM)\;or\;Co^{2+}(1.0mM)$ protected against the thermal denaturations of the enzyme activities. The michelis constant(Km) and $V_{max}$ values of the emzyme for D-glucose and D-xylose were 0.52M, $2.12{\mu}moles/ml{\cdot}min.\;and\;0.28M,\;0.65moles/ml{\cdot}min.$, respectively.

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