• 제목/요약/키워드: Inulin

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재조합 Saccharomyces cerevisiae에서 Inulinase의 발현과 국재성 (Expression and Localization of Inulinase in Recombinant Saccharomyces cerevisiae)

  • 남수완;우문희;김병문;정봉현;박영훈
    • 한국미생물·생명공학회지
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    • 제22권2호
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    • pp.152-157
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    • 1994
  • Inulinase of Kluyveromyces marxianus origin was produced by recombinant yeast Saccharomyces cerevisiae under the control of GAL1 promoter, to examine the expression and localization of inulinase in a repressed(galactose-free) or derepressed(galactose-containinga) medium. The inulinase gene(INU1A) was constitutively expressed at 6.7 units/ml in a repressed medium. When the cell started to utilize galactose in a derepressed medium, the INU1A gene began to be expressed, and the final expression level reached about 45 units/ml. According to be the nondenaturingPAGE analysis, inulinase produced by S. cerevisiae was found to be less glycosylated than the bakers yeast invertase. In addition, its glycosylation pattern was less heterogeneous than the K. marxianus inulinase. The supplementation of inulin or raffinose into the derepressed medium increased the cell growth rate, while the expression of INU1A was repressed. Regardless of the carbon sources examined, most of inulinase activity (more than 98%) was found in the extracellular medium, indicating excellent secretion efficiency.

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항진균성 항생물질을 생산하는 streptoverticillium sp. NA-4803의 분리 및 동정

  • 임대석;윤상군;이명섭;윤원호;김창한
    • 한국미생물·생명공학회지
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    • 제24권6호
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    • pp.664-670
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    • 1996
  • The aim of the present research program was to develop a strain of actinomycetes producing antifungal substance. Soil samples were collected from various sites in Korea and a number of actinomycetes were isolated from the soil samples by applying selective agar for actinomycetes. Among over 440 isolates, a strain (NA-4803) producing antifungal substance against Trichophyton spp. Nannizzia otae and Pyricularia oryzae was selected. The strain NA-4803 was identified as strain similar to Streptoverticillium blastmyceticum with respect to morphological and physiological characteristics, lecithinase and lipolytic activity, degradation of organic compounds, resistance to antibiotics and utilization of carbon and nitrogen sources. But it showed some differences such as positive reaction of nitrate reduction, negative reaction of L-tyrosine degradation, resistance to cephaloridine, and utilization of I -rhamnose and inulin. The strain NA-4803 was named as Streptoverticillium sp. NA-4803.

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Purification and Characterization of an Intracellular Inulinase from Bacillus sphaericus 188-1

  • Kim, Jae-Ho;Kwak, Yoon-Jin;Lee, Jong-Tae;Park, Shin-Yang;Lee, Jong-Soo
    • Preventive Nutrition and Food Science
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    • 제7권4호
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    • pp.421-426
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    • 2002
  • In order to obtain basal data for industrial application of inulinase from Bacillus sphaeicus 188-1, its intracellular inulinase was purified by ammonium sulfate fractionation and column chromatography on DEAE-Sephadex A-50 and Sephadex G-100. The enzyme was homogeneous as judged by SDS-polyacrylamide gel electrophoresis, with an apparent molecular weight of 29 kDa. Inulinase activity was optimal at pH 6.5 and 4$0^{\circ}C$. The enzyme activity was significantly inhibited by Cu$^{2+}$, Cd$^{2+}$ and Hg$^{2+}$. The inulinase exhibited an apparent Km value of 0.014% for inulin.

Yield of Jerusalem artichoke associated with different soil water content

  • Jong, Cheol;Han, Sangjun
    • 한국작물학회:학술대회논문집
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    • 한국작물학회 2017년도 9th Asian Crop Science Association conference
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    • pp.223-223
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    • 2017
  • This study aimed to determine the effect of organic matter content and water condition in soil on yield, carbohydrate, and inulin contents of two varieties of Jerusalem artichoke. The plants were grown with high and low organic soil either under irrigation or no irrigation in a randomized complete block design (RCBD) with three replications. In result, the yield of Jerusalem artichoke was higher about 7 kg in soil with high organic matter than in soil with low organic matter, while it was higher about 11 kg under the irrigation than under no irrigation. The yield of white variety was higher about 9 kg than that of purple variety. Under the irrigation, a 12 kg and 9 kg of higher yields were observed in the soil with high and low organic matter content, respectively, than under no irrigation.

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Exo-inulinase 생산 균주의 분리ㆍ동정 및 효소 생산의 최적화 (Isolation and identification of Exo-Inulinase Producing Bacterium and Optimization of the Enzyme Production)

  • 김병우;이경희
    • 생명과학회지
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    • 제9권1호
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    • pp.22-28
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    • 1999
  • A bacterium producing exo-inulinase was isolated from soil and identified Pseudomonas sp. and named as Pseudomonas sp. NO5. The optimal culture conditions for the efficient production of exo-inulinase from Pseudomonas sp. NO5 were obtained by cultivating with the medium 1$\%$ sucrose, 0.5$\%$ yeast extract, 0.5$\%$ $(NH_4)_2$$HPO_4$, 0.05$\%$ $MgSO_4$$7H_2$0, 0.001$\%$ and $FeSO_4$$7H_2$0 at $37^{\circ}C$ in initial pH 7.0 for 20 hours. The enzyme was induced maximally in the presence of sucrose or inulin at early stationary phase about 20 hour after cultivation.

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고려인삼(Panax ginseng C.A. Meyer) 잎 Invertase의 생화학적 특성 (Characteristics of Invertase from Korean ginseng (Panax ginseng C.A. Meyer) Leaf)

  • 김용환;심우만
    • 한국식품영양학회지
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    • 제5권2호
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    • pp.144-149
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    • 1992
  • Invertase was extracted from Korean ginseng(Panax ginseng C. A. Meyer) leaf with deionized water, and then prepared by ammonium sulfate(0.4~0.6 Sat.) fractionation, the enzymological properties of the invertase were investigated, and the results obtained were as follows. The optimum pH and temperature of the enzyme were pH 6.0 and 4$0^{\circ}C$ respectively. The enzyme was stable in the pH range of pH 6.0 to 8.0, and at the temperature below 4$0^{\circ}C$. The enzyme was inactivated completely by the treatment with some proteases(pepsin, trypsin, papain and ficin) and protein denaturants(8M urea and 6M guanidine-HCI), but not with glycosidases (a-amylase, $\beta$-amylase and glucoamylase). The enzyme catalyzed specifically the hydrolization of the $\beta$-fructofuranosides such as sucrose and inulin.

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수지 촉매에 의한 Polyfructan의 가수분해 (Hydrolysis of Polyfructan by Resin Catalysts)

  • 김성배;이동근최주홍
    • KSBB Journal
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    • 제5권4호
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    • pp.397-402
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    • 1990
  • Hydrolysis of inulin was investigated employing various commercially available resin catalysts for the production of high grade fructose syrup. The particle size and porosity of the resin significantly affected the distribution of the products, indicating that the intraparticle diffusion of reactants controls thc selectivity as well as the reaction rate. To confirm the effect of the intraparticle diffusion, two different types of resin catalysts were prepared: the one having sulfonic acid group distributed uniformly throughout genular microparticles (A-type) and the other having sulfonic acid group located mainly at the exterior surface of genular microparticles (E-type). The results were found that the reaction rate and the selectivity of the E-type catalyst were higher than those of the A-type catalyst.

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Saponin isolated from Platycodon grandiflorum induces cell cycle arrest in hepatic stellate cells

  • Lee, Kyung-Jin;Shin, Dong-Weon;Chung, Young-Chul;Kim, Young-Sup;Ryu, Si-Yung;Roh, Sung-Hwan;Cho, Young-Soo;Jeong, Hye-Gwang
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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    • pp.103.3-104
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    • 2003
  • Activation of hepatic stellate cell has been identified as a critical step in hepatic fibrogenesis and is regulated by several factors including cytokines and oxidative stress. In this study, we assayed effects of saponin (CKS), inulin (CKI) and oligo-sugars (CKO) isolated from Platycodon grandiflorum A. DC, changkil (CK) on experimental cell cycle arrest and apoptosis in hepatic stellate cell line (HSC-T6). CKS induced cell arrest at G$_1$. CKS also reduced intercellular reactive oxygen species and collagen synthesis in hydrogen peroxide-induced oxidative stress and acetaldehyde-stimulated collagen synthesis, respectively, in HSC-T6 cells. (omitted)

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고려인삼(Panax ginseng) Invertase의 정제와 그 특성 (Purification and Characterization of Invertase from Korean Ginseng Panax ginseng)

  • 김용환;김병묵
    • Journal of Ginseng Research
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    • 제14권1호
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    • pp.14-20
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    • 1990
  • In An invertase (EC 3.2.1.26) was extracted from Korean giseng (Panax ginseng C.A. Meyer) with distilled tvater The ginseng invertase was purified about 62.6 folds purified by procedures including ammonium sulfate fractionation , DEAE-cellulofine chromatography and gelfiltrations through Sephadex G-75 and the recovery of enzyme activity was 11.1%. The homogeneity of the purified enzyme was probed by polyacrylamide gel disc electrophoresis. The purifled enzyme was divided into two different subunits by treating with a mixture of SDS and 2-mercautoethanol, and the molecular weight of the large subunit was estimatedtobe 116,000 and that of the small one to be 14,000. The optimal VH and temperature of the enzyme were pH 6 and 45$^{\circ}C$, respectively. The enzyme hydrolyzed specifically the hydrolyzation of the -fructofuranosides such as sucrose, raffinose and inulin. The Km values of the enzyme for sucrose and raffinose were determined to be 0.85 and 0.6 mM, respectively.

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Purification and Characterization of Cycloinulooligosaccharide Fructanotransferase from Bacillus macerans CFC1

  • Kim, Hwa-Young;Choi, Yong-Jin
    • Journal of Microbiology and Biotechnology
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    • 제8권3호
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    • pp.251-257
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    • 1998
  • Cycloinulooligosaccharide fructanotransferase (CFTase) which produces cyclofructan from inulin was purified 332-fold from a culture broth of Bacillus macerans CFCl. The molecular mass of the CFTase was estimated to be 110 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indicating that the enzyme has a monomer structure. The maximal level of enzyme activity was observed at pH 7.5 and $45^{\circ}C$. The enzyme was stable in the pH range 6.0 to 9.5, and at temperatures up to $45^{\circ}C$ for 1 h. The enzyme activity was completely inhibited in the presence of 0.5 mM $Ag^+\;or\;Cu^2+$ ion. None of sucrose (GF), l-kestose (GF2), or nystose (GF3) were found to be substrates for the CFTase, but inulooligosaccharides larger than nystose were attacked by the enzyme. The CFTase catalyzes not only the cyclization as the major reaction, but also disproportionation and coupling reactions involving intermolecular transfructosylation in the same manner as cyclodextrin glucanotransferase (CGTase) (EC 2.4.1.19).

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