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T : 목차정보

Journal of microbiology and biotechnology 13건

  1. [국내논문]   Large-scale Recovery of Recombinant Protein Inclusion Bodies Expressed in Escherichia coli   피인용횟수: 2

    Middelberg. Anton P.J. (Department of Chemical Engineering, The University of Adelaide)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 225 - 231 , 1996 , 1017-7825 ,

    초록

    The production of recombinant proteins in Escherichia coli often leads to the formation of an intracellular inclusion body. Key process steps that can determine the economics of large-scale protein production from inclusion bodies are fermentation, inclusion body recovery, and protein refolding. Compared with protein refolding and fermentation, inclusion body recovery has received scant research attention. Nevertheless, it can control the final product yield and hence process cost for some products. Optimal separation of inclusion bodies and cell debris can also aid subsequent operations by removing contaminant particulates that foul chromatographic resins and contain antigenic pyrogens. In this review, the properties of inclusion bodies and cellular debris are therefore examined. Attempts to optimise the centrifugal separation of inclusion bodies and debris are also discussed.

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  2. [국내논문]   The Growth Yield of Desulfovibrio desulfuricans M6 on Different Substrates  

    Park, Doo-Hyun (Department of Biological Engineering, Seo Kyung University ) , Shin, Chul-Su (Han Hyo Institute of Science ) , Kim, Byung-Hong (Environmental Research Center, Korea Institute of Science and Technology ) , Shin, Pyung-Kyun (Environmental Research Center, Korea Institute of Science and Technology)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 232 - 237 , 1996 , 1017-7825 ,

    초록

    Growth yield of Desulfovibrio desulfuricans M6 was measured using different substrates. The cell yield of fermentative growth on pyruvate was 6.22 g cell $mol^{-l}$ pyruvate. Since 1 ATP is available from substrate-level phosphorylation from the oxidation of pyruvate to acetate, $Y_{ATP}$ of the bacterium should be the same as $Y_{pyruvate}$ (6.22 g cell $mol^{-l}$ ATP). The cell yields of the bacterium on different electron donors were measured with sulfate as the electron acceptor. Cell yields on lactate, pyruvate and $H_2$ were 9.39, 13.76 and 8.45 g cell $mol^{-l}$ substrate, respectively. From these figures ATP available from electron-transport phosphorylation (ETP) of the electron donors used was calculated. ATP produced by ETP of each electron donnor were 1.71 from pyruvate, 1.51 from lactate and 1.76 from $H_2$ . These values show that electrons from the oxidation of lactate to pyruvate are consumed to reduce sulfate through a reverse electron transport mechanism requiring 0.2 ATP for each pair of electrons. Based on these results, discussions are made on the electron transport mechanism in the bacterium.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  3. [국내논문]   Purification and Properties of $\gamma$-Glutamyl Transpeptidase from Bacillus sp. KUN-17   피인용횟수: 1

    Hwang, Se-Young (Department of Biotechnology(Seochang) Korea University ) , Ryang, Jun-Hwan (Department of Biotechnology(Seochang) Korea University ) , Lim, Wang-Jin (Institute of Biotechnology(Anam), Korea University ) , Yoo, Ick-Dong (Korea Research Institute of Bioscience and Biotechnology, KIST ) , Kunio Oishi (Department of Agricultural Chemistry, Nihon University)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 238 - 244 , 1996 , 1017-7825 ,

    초록

    $\gamma$ -Glutamyl transpeptidase ( $\gamma$ -GTP; EC 2.3.2.2) present in the culture filtrate of Bacillus sp. KUN-17 was purified 400-fold through a consecutive procedure including organic precipitation and column chromatography. The enzyme has an estimated molecular weight of 70, 000 and consists of hetero-subunits with molecular weights of 42, 000 and 22, 000. In vitro optimal conditions for those transfer and hydrolysis reactions appeared to be pH 7.0 at $50^{\circ}C$ and pH 8.4 at $40^{\circ}C$ , respectively. The denatured enzyme recovered most of its $\gamma$ -GTP activity by removing detergents such as sodium dodecyl sulfate (SDS) or urea with dialysis. The enzyme showed higher affinities against a number of amino acids as $\gamma$ -glutamyl acceptors than glycylglycine in the following order: L-valine, L-methionine, L-glutamic acid or L-as-paragine, L-alanine. Also, it was shown that L-glutamine was the most suitable $\gamma$ -glutamyl donor for the transfer reaction among those tested. Amino acids generally inhibited the enzyme activity for the transfer reaction, but not for the hydrolysis reaction.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  4. [국내논문]   Structure Determination and Biological Activities of Elaiophylin Produced by Streptomyces sp. MCY-846  

    Lee, S.-Y. ; Kim, M.-S. ; Kim, H.-S. ; Kim, Y.-H. ; Hong, S.-D. ; Lee, J.-J.
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 245 - 249 , 1996 , 1017-7825 ,

    초록

    $\gamma$ -Glutamyl transpeptidase ( $\gamma$ -GTP; EC 2.3.2.2) present in the culture filtrate of Bacillus sp. KUN-17 was purified 400-fold through a consecutive procedure including organic precipitation and column chromatography. The enzyme has an estimated molecular weight of 70, 000 and consists of hetero-subunits with molecular weights of 42, 000 and 22, 000. In vitro optimal conditions for those transfer and hydrolysis reactions appeared to be pH 7.0 at $50^{\circ}C$ and pH 8.4 at $40^{\circ}C$ , respectively. The denatured enzyme recovered most of its $\gamma$ -GTP activity by removing detergents such as sodium dodecyl sulfate (SDS) or urea with dialysis. The enzyme showed higher affinities against a number of amino acids as $\gamma$ -glutamyl acceptors than glycylglycine in the following order: L-valine, L-methionine, L-glutamic acid or L-as-paragine, L-alanine. Also, it was shown that L-glutamine was the most suitable $\gamma$ -glutamyl donor for the transfer reaction among those tested. Amino acids generally inhibited the enzyme activity for the transfer reaction, but not for the hydrolysis reaction.

    원문보기

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    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  5. [국내논문]   The Slow and Tight Binding of MR-387A to Aminopeptidase N  

    Chung, M.-C. ; Chun, H.-K. ; Lee, H.-J. ; Lee, C.-H. ; Kim, S.-I. ; Kho, Y.-H.
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 250 - 254 , 1996 , 1017-7825 ,

    초록

    $\gamma$ -Glutamyl transpeptidase ( $\gamma$ -GTP; EC 2.3.2.2) present in the culture filtrate of Bacillus sp. KUN-17 was purified 400-fold through a consecutive procedure including organic precipitation and column chromatography. The enzyme has an estimated molecular weight of 70, 000 and consists of hetero-subunits with molecular weights of 42, 000 and 22, 000. In vitro optimal conditions for those transfer and hydrolysis reactions appeared to be pH 7.0 at $50^{\circ}C$ and pH 8.4 at $40^{\circ}C$ , respectively. The denatured enzyme recovered most of its $\gamma$ -GTP activity by removing detergents such as sodium dodecyl sulfate (SDS) or urea with dialysis. The enzyme showed higher affinities against a number of amino acids as $\gamma$ -glutamyl acceptors than glycylglycine in the following order: L-valine, L-methionine, L-glutamic acid or L-as-paragine, L-alanine. Also, it was shown that L-glutamine was the most suitable $\gamma$ -glutamyl donor for the transfer reaction among those tested. Amino acids generally inhibited the enzyme activity for the transfer reaction, but not for the hydrolysis reaction.

    원문보기

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    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

    Fig. 1 이미지
  6. [국내논문]   Growth and ?Glucosidase Activity of Bifidobacterium  

    Choi, Y.-J. ; Kim, C.-J. ; Park, S.-Y. ; Ko, Y.-T. ; Jeong, H.-K. ; Ji, G.-E.
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 255 - 259 , 1996 , 1017-7825 ,

    초록

    $\gamma$ -Glutamyl transpeptidase ( $\gamma$ -GTP; EC 2.3.2.2) present in the culture filtrate of Bacillus sp. KUN-17 was purified 400-fold through a consecutive procedure including organic precipitation and column chromatography. The enzyme has an estimated molecular weight of 70, 000 and consists of hetero-subunits with molecular weights of 42, 000 and 22, 000. In vitro optimal conditions for those transfer and hydrolysis reactions appeared to be pH 7.0 at $50^{\circ}C$ and pH 8.4 at $40^{\circ}C$ , respectively. The denatured enzyme recovered most of its $\gamma$ -GTP activity by removing detergents such as sodium dodecyl sulfate (SDS) or urea with dialysis. The enzyme showed higher affinities against a number of amino acids as $\gamma$ -glutamyl acceptors than glycylglycine in the following order: L-valine, L-methionine, L-glutamic acid or L-as-paragine, L-alanine. Also, it was shown that L-glutamine was the most suitable $\gamma$ -glutamyl donor for the transfer reaction among those tested. Amino acids generally inhibited the enzyme activity for the transfer reaction, but not for the hydrolysis reaction.

    원문보기

    원문보기
    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

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  7. [국내논문]   Identification and Fermentation of a Streptomyces Producing Aurodox Group Antibiotics  

    Kim, Si-Kwan (Korea Ginseng and Tobacco Research Institute ) , Yeo, Woon-Hyung (Korea Ginseng and Tobacco Research Institute ) , Kim, Sang-Seock (Korea Ginseng and Tobacco Research Institute)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 260 - 264 , 1996 , 1017-7825 ,

    초록

    An isolate, 90-GT-129 was found to produce antibiotics with a selective inhibitory activity against Streptococcus pyogenes and Xanthomonas sp. The isolate formed a gray spiral aerial spore mass with smooth surface. Analysis of the cell wall acid hydrolysate of the isolate revealed presence of LL-di-aminopimelic acid, which indicates that the isolate belongs to a cell wall type Ⅰ actinomycetes. Cultural and physiological characteristics of the isolate placed it in Streptomyces rochei synonym cluster. A comparison of the isolate with 26 reference strains of Streptomyces rochei synonym demonstrated differences in physiological and cultural characteristics.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

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  8. [국내논문]   Isolation, Physico-chemical Properties and Biological Activity of Aurodox Group Antibiotics  

    Kim, Si-Kwan (Korea Ginseng and Tobacco Research Institute ) , Yeo, Woon-Hyung (Korea Ginseng and Tobacco Research Institute ) , Kim, Sang-Seock (Korea Ginseng and Tobacco Research Institute)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 265 - 269 , 1996 , 1017-7825 ,

    초록

    An isolate of Streptomyces rochei synonym was found to produce antibiotics with narrow anti-microbial spectrum against Streptococcus and Xanthomonas sp. Among the antibiotic complex produced by the strain, the main active compound was isolated, and its physico-chemical properties and biological activities were investigated. Molecular weight of the compound was determined to be ${[M+H]}^+$ 797 (FAB-MS). UV, $^1H \;and\;^{13}C$ NMR, and IR spectra suggested that the compound is a kirromycin-like aurodox group antibiotic. However, the anti-microbial spectrum of the main compound was slightly different from that of kirromycin. In addition, it was newly found that kirromycin showed a selective anti-microbial activity against Streptococcus pyogenes and phytopathogenic Xanthomonas sp.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  9. [국내논문]   Isolation of Leuconostoc mesenteroides subsp. mesenteroides DU-0608 with Antibacterial Activity from Kimchi and Characterization of Its Bacteriocin   피인용횟수: 5

    Cha, Dong-Soo (Department of Food Technology, Dongguk University ) , Ha, Duk-Mo (Department of Food Technology, Dongguk University)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 270 - 277 , 1996 , 1017-7825 ,

    초록

    A bacteriocin-producing strain, DU-0608, was isolated from Kimchi and identified as Leuconostoc mesenteroides subsp. mesenteroides. The bacteriocin from isolate was inhibitory against Listeria monocytogenes, Micrococcus luteus and several strains of lactic acid bacteria. The bacteriocin was inactivated by pepsin, trypsin, $\alpha$ -chymotrypsin, protease, $\alpha$ -amylase and lipase, but not by catalase or by heating at $100^{\circ}C$ for 60 min. The molecular weight of the bacteriocin was estimated approximately 6 kDa. The inhibitory effect was bactericidal and rapid. Following treatment with isolate bacteriocin, cells of indicator strain (Lactobacillus sake JCM 1157) were damaged at the end regions of the cell wall, whereas the cells treated with nisin were damaged at many places around the cell wall.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  10. [국내논문]   Aroma Components of Traditional Korean Soy Sauce and Soybean Paste Fermented with the Same Meju  

    Seo, Jae-Soon (Dept. of Applied Microbiology, Yeungnam University ) , Chang, Ho-Geun (Dept. of Applied Microbiology, Yeungnam University ) , Ji, Won-Dae (Dept. of Applied Microbiology, Yeungnam University ) , Lee, Eun-Ju (Dept. of Applied Microbiology, Yeungnam University ) , MYEONG-RAK-CHOI (Dept. of Biological Engineering, Yosu Fisheries National University ) , HAENG-JA-KIM (Dept. of Economics Education, Kyeongsang National University)
    Journal of microbiology and biotechnology v.6 no.4 ,pp. 278 - 285 , 1996 , 1017-7825 ,

    초록

    We identified volatile components of traditional Korean soy sauce and soybean paste which had been manufactured with the same traditional Meju with a view to improving the quality of traditional Korean soy sauce and soybean paste. All of the volatile components were extracted by simultaneous steam distillation-extraction (SDE) apparatus. To obtain more detailed information, whole volatile components were separated into fractions. The volatile components of the whole and of each fraction were identified by GC-mass and Kovat's retention index. Sixty two and eighty six components were identified in traditional Korean soy sauce and soybean paste, respectively. Many aroma components of traditional Korean soy sauce differ from those of traditional Korean soybean paste. It was confirmed that many aroma components of traditional Korean soy sauce and soybean paste are completely different from those of Japanese fermented soy sauce (Shoyu) and soybean paste (Miso).

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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