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Journal of microbiology and biotechnology 11건

  1. [국내논문]   Lysine $\varepsilon$-Aminotransferase, the Initial Enzyme of Cephalosporin Biosynthesis in Actinomycetes   피인용횟수: 2

    Rius, Nuria (Fermentation Microbiology Laboratory, Biology Department, Massachusetts Institute of Technology ) , Demain, Arnold L. (Fermentation Microbiology Laboratory, Biology Department, Massachusetts Institute of Technology)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 95 - 100 , 1997 , 1017-7825 ,

    • 원문 

    초록

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  2. [국내논문]   Strain Improvement for Enhanced Production of Streptokinase and Streptodornase in Streptococcus sp  

    Hyun, H.-H. ; Lee, Y.-B. ; Song, K.-H. ; Jeon, J.-Y. ; Lee, H.-H.
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 101 - 106 , 1997 , 1017-7825 ,

    초록

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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.

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  3. [국내논문]   Purification and Characterization of Antifungal Chitinase from Pseudomonas sp. YHS-A2   피인용횟수: 5

    Lee, Han-Seung (Department of Food & Biotechnology, College of Engineering, Yonsei University, and Bioproducts Research Center ) , Lee, Hyun-Jung (Department of Food & Biotechnology, College of Engineering, Yonsei University, and Bioproducts Research Center ) , Choi, Sung-Won (Department of Food & Biotechnology, College of Engineering, Yonsei University, and Bioproducts Research Center ) , Her, Song (Department of Food & Biotechnology, College of Engineering, Yonsei University, and Bioproducts Research Center ) , Oh, Doo-Hwan (Department of Food & Biotechnology, College of Engineering, Yonsei University, and Bioproducts Research Center)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 107 - 113 , 1997 , 1017-7825 ,

    초록

    A strain producing a high amount of chitinase was isolated from soil, identified as Pseudomonas sp., and tentatively named Pseudomonas sp. YHS-A2. An extracellular chitinase of Pseudomonas sp. YHS-A2 was purified according to the procedure of ammonium sulfate saturation, affinity adsorption, Sephadex G-100 gel filtration and Phenyl-sepharose CL-4B hydrophobic interaction column chromatography. The molecular weight of the purified enzyme was estimated to be 55 kDa on SDS-PAGE was confirmed by active staining. Optimal pH and temperature of the enzyme are pH 7.0 and $50^{\circ}C$ , respectively, and the enzyme is stable between pH 5.0 and 8.0 and below $50^{\circ}C$ . The main products of colloidal chitin by the chitinase were N-acetyl-D-glucosamine and N,N'-diacetylchitobiose both of which were detected by HPLC analysis. The enzyme is supposed to be a random-type endochitinase which can degrade any position of ${\beta}$ -l,4-linkages of chitin and chitooligosaccharides. The chitinase inhibited the growth of some phytopathogenic fungi, Fusarium oxysporum, Botrytis cineria, and Mucor rouxii and these antifungal effects were thought to be due to the characteristics of endochitinase.

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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.

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  4. [국내논문]   Characterization of an Endoxylanase Produced by an Isolated Strain of Bacillus sp.   피인용횟수: 1

    Lee, Jay-J. (Department of Biological Sciences, Korea Advanced Institute of Science and Technology ) , Hahm, Kyoung-Soo (Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, Korea Institute of Science and Technology ) , Lee, Ki-Young (Department of Food and Nutrition, Hoseo University ) , Lee, Sung-Taik (Department of Biological Sciences, Korea Advanced Institute of Science and Technology)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 114 - 120 , 1997 , 1017-7825 ,

    초록

    Microorganisms producing xylanase were screened for the enzymatic production of xylo-oligo saccharides from xylan. One of the bacteria isolated from compost produced an endoxylanase extracellularly. The bacterium was identified as Bacillus sp. according to its taxonomic characteristics examined. Xylanase production reached upto 5 U/ml after 22 h of culture in LB medium at $30^{\circ}C$ . The xylanase was purified by ammonium sulfate precipitation and gel filtration. The molecular weight of the xylanase was estimated to be 20,400 by SDS-PAGE. Optimal temperature and pH for the xylanase activity was $60^{\circ}C$ and 6.5, respectively. The enzyme was stable at temperatures upto $40^{\circ}C$ and pH values from 4 to 10. The xylanase was completely inhibited by the addition of 2 mM mercury ion. Apparent $K_m$ and $V_max$ values for oat spelt xylan were 9.2 mg/ml and 1954 U/mg protein, respectively. For birchwood xylan, the values were 6.3 mg/ml and 1009 U/mg protein. The predominant products of the xylan hydrolysis were xylobiose, xylotriose and xylotetraose, indicating that the enzyme is an endoxylanase. Upto $85{\%}$ of the initially added enzyme (2 U/ml) was bound to 50 mg/ml of the insoluble fraction of oat spelt xylan after incubation at $30^{\circ}C$ for 30 min.

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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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  5. [국내논문]   Purification and Characterization of an Inulin Fructotransferase from Flavobacterium sp. LC-413  

    Cho, Chul-Man (Department of Microbiology, College of Natural Sciences, Pusan National University ) , Lee, Sang-Ok (Department of Microbiology, College of Natural Sciences, Pusan National University ) , Hwang, Ji-Sook (Department of Microbiology, College of Natural Sciences, Pusan National University ) , Jang, Kyung-Lip (Department of Microbiology, College of Natural Sciences, Pusan National University ) , Lee, Tae-Ho (Department of Microbiology, College of Natural Sciences, Pusan National University)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 121 - 126 , 1997 , 1017-7825 ,

    초록

    A bacterial strain LC-413, producing an extracellular inulin fructotransferase (depolymerizing) which converts inulin into di-D-fructofuranose dianhydride (DFAIII), was isolated from soil. Inulin fructotransferase from the isolate identified as a strain Flabobacterium sp. was purified from the culture broth by ammonium sulfate precipitation, followed by column chromatograpies on DEAE-Toyopearl 650 M and phenyl-Toyopearl 650 M. The purified enzyme gave a single band on an electrophoretic disc-gel. The molecular weight of the enzyme was estimated to be 44, 000 Da by SDS-polyacrylamide gel electrophoresis, and 45, 000 Da by gel filtration, suggesting the monomeric state of the enzyme. The isoelectric point of the enzyme was about pH 4.5. The optimal pH and temperature for the enzyme reaction were 6.0 and $50^{\circ}C$ , respectively. The purified enzyme digested inulin into di-D-fructofuranose-l, 2': 2, 3'-dianhydride, confirming the enzyme was an inulin fructotransferase (inulinase II).

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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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  6. [국내논문]   Effects of Amino Acids, Carbohydrates and Phosphorus Sources on Growth and Alkaline Phosphatase Activity of the Marine Cyanobacterium Anabaena sp. Strain CA  

    Singh, Jeet Bahadur (Centre of Advanced Study in Botany, Banaras Hindu University ) , Vyas, Deepak (Centre of Advanced Study in Botany, Banaras Hindu University ) , Kumar, Har Darshan (Centre of Advanced Study in Botany, Banaras Hindu University)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 127 - 131 , 1997 , 1017-7825 ,

    초록

    Alkaline phosphatase (APase) was found to be inducible in Anabaena sp. strain CA Growth was less than control in presence of most amino acids except glycine and serine, but most amino acids enhanced APase activity. Highest APase activity was recorded in tyrosine supplemented culture followed by hydroxyproline, cystein, valine and glutamic acid. Threonine supplemented material showed lowest APase level (1.8 nmol/mg protein/min). Lactose, glucose, sodium pyruvate and succinate stimulated growth but not APase activity. APase activity was high in the presence of sucrose, mellibiose, mannitol, arabinose, maltose and sorbose, even though the growth in these supplements was less than in control. Organic phosphate sources supported good growth of the organism. Best growth occurred in presence of inorganic phosphate, adenosine diphosphate, fructose 1,6-diphosphate or ribulose 1,5-diphosphate, followed by other phosphorus sources tested. APase activity in presence of any of the organic phosphate sources was 3 to 5 fold low as compared to phosphate limited culture. Also, there was no APase activity in cultures grown on inorganic phosphate. These data indicate that most amino acids and a few carbohydrates (sucrose, mellibiose, arabinose and sorbose) are suitable for APase production. Lactose, glucose, pyruvate or succinate may be used as a carbon source during photoheterotrophic growth of the cyanobacterium. Glycine and serine are preferred nitrogen sources for its growth. Phosphate repressible APase activity has been found in Anabaena sp. strain CA.

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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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  7. [국내논문]   Design and Expression of High Nutritional Peptide (HEAAE) in E. coli  

    Kim, Jae-Ho (Graduate School of Biotechnology, Korea University ) , Lee, Chang-Kook (Utilization Research Lab, National Fisheries Research and Development Agency ) , Hong, Bum-Shik (Graduate School of Biotechnology, Korea University)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 132 - 137 , 1997 , 1017-7825 ,

    초록

    A novel protein (HEAAE, High Essential Amino Acid Encoding Protein), rich in essential amino acids ( $75{\%}$ of total), was designed and constructed in our laboratory. The designed peptides were analyzed by SYBLE and stable secondary and tertiary structures were predicted. The monomeric form (HEAAE-1) of the protein consists of 20 amino acid residues with four additional amino acids comprising a potential ${\beta}$ -turn (HEAAE-4). Size exclusion analysis demonstrated that the monomer is self-aggregates in aqueous solution to form higher ordered multimeric structures, which are very reminiscent of natural plant storage proteins. The DNA encoding this amino acid sequence was synthesized, and from this monomeric gene fragment (heaae-1), the stable tetrameric form of the gene (heaae-4) was generated by subcloning into the E. coli expression vector pKK223-3. A clear 6 kDa polypeptide band corresponding to the molecular weight of the dimeric form (HEAAE-2) was detected. The smeared band which appeared around the molecular weight corresponding to HEAAE-4 of 11 kDa suggested that the tetramer form of this protein might be processed into smaller size products.

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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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  8. [국내논문]   Expression of de novo Designed High Nutritional Peptide (HEAAE) in Tobacco   피인용횟수: 1

    Kim, Jae-Ho (Graduate School of Biotechnology, Korea University ) , Lee, Chang-Kook (Utilization Research Lab, National Fisheries Research and Development Agency ) , Hong, Bun-Shik (Graduate School of Biotechnology, Korea University)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 138 - 143 , 1997 , 1017-7825 ,

    초록

    We have designed and constructed a gene encoding novel high essential amino acid encoding protein(HEAAE). The resultant DNA fragment was tested for in vitro and in vivo expression and then cloned into plant expression vector pBI121, under the control of the cauliflower mosaic virus 35S promoter. Agrobacterium tumefaciens, strain LBA4404, was subsequently transformed with this new construct and Nicotiana tabacum var. Xanthi transgenic plants were obtained. DNA analysis by Southern procedure confirmed the presence of the multi-copy number of genes in the transformed plants. Analysis of RNA and protein synthesized in these transgenic plants demonstrated the stable expression of this gene.

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

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  9. [국내논문]   An Outer Membrane Protein Preparation as a Vaccine against Pseudomonas aeruginosa Infection   피인용횟수: 1

    Park, Wan-Je (Research and Development Center, Cheiljedang Inc. ) , Cho, Yang-Je (Research and Development Center, Cheiljedang Inc. ) , Ahn, Dong-Ho (Research and Development Center, Cheiljedang Inc. ) , Jung, Sang-Bo (Research and Development Center, Cheiljedang Inc. ) , Lee, Na-Gyong (Research and Development Center, Cheiljedang Inc. ) , Kim, Hyun-Su (Research and Development Center, Cheiljedang Inc. ) , Hahm, Kyung-Soo (Research Institute of Bioscience and Biotechnology, KIST ) , Kim, Yu-Sam (Department of Biochemistry, College of Science, Yonsei University)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 144 - 150 , 1997 , 1017-7825 ,

    초록

    We developed a simple and efficient method to prepare a Pseudomonas vaccine of outer membrane (OM) proteins free from lipopolysaccharide (LPS). A three step purification process including extraction, ultrafiltration and ultracentrifugation effectively removed LPS from the OM protein fraction. Approximately 2 mg of the OM proteins was obtained from 1 g of wet cell. LPS contaminant in the vaccine preparation was less than 0.003% (w/w) of protein and protease activity was not detectable. To achieve a wide range of protection, OM proteins prepared from four attenuated P. aeruginosa strains were mixed in equal amounts and used as a vaccine, which elicited in rabbits a high titer of antibody reactive to all of the seven Fisher types. The antisera from the immunized rabbit had a strong reactivity to vaccine proteins larger than 25 kDa. In a burned mouse infection model, immunization with the vaccine significantly enhanced bacterial clearance in the Pseudomonas infected skin. The vaccination also provided mice an excellent protection against Pseudomonas infection (11, 16). Data on antigenicity, mutagenicity, acute, subacute toxicity and pharmacological tests confirmed the safety of the vaccine (1, 3, 10, 12, 17). These data demonstrate that this method can be applied to manufacture a bacterial vaccine of OM proteins with safety and prophylactic efficacy at a practical low cost.

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

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  10. [국내논문]   Hydrolysis of Olive Oil by Lipase, Immobilized on Hydrophobic Support   피인용횟수: 4

    Jung, Ju-Young (Department of Biological Engineering, Inha University ) , Yun, Hyun-Shik (Department of Biological Engineering, Inha University ) , Kim, Eun-Ki (Department of Biological Engineering, Inha University)
    Journal of microbiology and biotechnology v.7 no.2 ,pp. 151 - 156 , 1997 , 1017-7825 ,

    초록

    Two commercially available lipases, Lipase OF (non-specific lipase from Candida rugosa) and Lipolase 100T (1, 3-specific lipase from Aspergillus niger), were immobilized on insoluble hydrophobic support HDPE (high density polyethylene) by the physical adsorption method. Hydrolysis performance was enhanced by mixing a non-specific Lipase OF and a 1, 3-specific Lipolase 100T at a 2 : 1 ratio. The results also showed that the immobilized lipase maintained its activity at broader temperature ( $25~55^{\circ}C$ ) and pH (4-8) ranges than soluble lipases. In the presence of organic solvent (isooctane), the immobilized lipase retained most of its activity in upto 12 runs of hydrolysis experiment. However, without organic solvent in the reaction mixture, the immobilized lipase maintained most of its activity even after 20 runs of hydrolysis experiment.

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