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Biotechnology and bioprocess engineering : Bbe 16건

  1. [국내논문]   Rapid Selection of Multiple Gene Integrant for the Production of Recombinant Hirudin in Hansenula polymorpha  

    Kim Hwa Young (Korea Research Institute of Bioscience and Biotechnology ) , Sohn Jung Hoon (Korea Research Institute of Bioscience and Biotechnology ) , Kim Chul Ho (Korea Research Institute of Bioscience and Biotechnology ) , Rao K. Jagannadha (Korea Research Institute of Bioscience and Biotechnology ) , Choi Eui Sung (Korea Research Institute of Bioscience and Biotechnology ) , Kim Myung Kuk (Central Research Institute, Dong Kook Pharmaceutical Co. Ltd. ) , Rhee Sang Ki (Korea Research Institute of Bioscience and Biotechnology)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 1 - 6 , 2000 , 1226-8372 ,

    초록

    For the rapid selection of higher recombinant hirudin producing strain in a methylotrophic yeast Hansenula polymorpha, a multiple gene integration and dose-dependent selection vector, based on a telomere-associated ARS and a bacterial aminoglycoside 3-phosphotransferase (aph) gene, was adopted. Two hirudin expression cassettes (HV1 and HV2) were constructed using the MOX promoter of H. polymorpha and the mating factor $\alpha$ secretion signal of S. cerevisiae. Multiple integrants of a transforming vector containing hirudin expression cassettes were easily selected by using an antibiotic, G418. Hirudin expression level and integrated plasmid copy number of the tested transformants increased with increasing the concentration of G418 used for selection. The expression level of HV1 was consistently higher than that of HV2 under the similar conditions, suggesting that the gene context might be quite important for the high-level gene expression in H. polymorpha. The highest hirudin producing strain selected in this study produced over 96 mg/L of biologically active hirudin in a 500-mL flask and 165 mg/L in a 5-L fermentor.

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  2. [국내논문]   Expression of mouse α-amylase gene in methylotrophic yeastPichia pastoris  

    Uehara, Hiroyuki , Du Choi, Bok , Park, Enoch Y. , Okabe, Mitsuyasu
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 7 - 12 , 2000 , 1226-8372 ,

    초록

    For the rapid selection of higher recombinant hirudin producing strain in a methylotrophic yeast Hansenula polymorpha, a multiple gene integration and dose-dependent selection vector, based on a telomere-associated ARS and a bacterial aminoglycoside 3-phosphotransferase (aph) gene, was adopted. Two hirudin expression cassettes (HV1 and HV2) were constructed using the MOX promoter of H. polymorpha and the mating factor $\alpha$ secretion signal of S. cerevisiae. Multiple integrants of a transforming vector containing hirudin expression cassettes were easily selected by using an antibiotic, G418. Hirudin expression level and integrated plasmid copy number of the tested transformants increased with increasing the concentration of G418 used for selection. The expression level of HV1 was consistently higher than that of HV2 under the similar conditions, suggesting that the gene context might be quite important for the high-level gene expression in H. polymorpha. The highest hirudin producing strain selected in this study produced over 96 mg/L of biologically active hirudin in a 500-mL flask and 165 mg/L in a 5-L fermentor.

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  3. [국내논문]   Expression of Mouse $\alpha-Amylase$ Gene in Methylotrophic Yeast Pichia pastoris  

    Uehara Hiroyuki (Lab. of Biotechnology, Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University ) , Choi Du Bok (Institute of Life Science, Chosun University ) , Park Enoch Y. (Lab. of Biotechnology, Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University ) , Okabe Mitsuyasu (Lab. of Biotechnology, Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 7 - 12 , 2000 , 1226-8372 ,

    초록

    The expression of the mouse $\alpha-amylase$ gene in the methylotrophic yeast, P pastoris was investigated. The mouse $\alpha-amylase$ gene was inserted into the multi-cloning site of a Pichi a expression vector, pPIC9, yielding a new expression vector pME624. The plasmid pME624 was digested with SalI or BglII, and was introduced into P. pastoris strain GSl15 by the PEG1000 method. Fifty-three transformants were obtained by the transplacement of pME624 digested with SaiII or BglII into the HIS4locus $(38\;of\;Mut^+\;clone)$ or into the AOX1 locus $(15\;of\;Mut^s\;clone)$ . Southern blot was carried out in 11 transformants, which showed that the mouse $\alpha-amylase$ gene was integrated into the Pichia chromosome. When the second screening was performed in shaker culture, transformant G2 showed the highest $\alpha-amylase$ activity, 290 units/ml after 3-day culture, among 53 transformants. When this expression level of the mouse $\alpha-amylase$ gene is compared with that in recombinant Saccharomyces cerevisiae harboring a plasmid encoding the same mouse $\alpha-amylase$ gene, the specific enzyme activity is eight fold higher than that of the recombinant S. cerevisiae.

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  4. [국내논문]   Simple Purification of Escherichia coli-Derived Recombinant Human Interleukin-2 Expressed with N-terminus Fusion of Glucagon   피인용횟수: 1

    Won Hye-Soon (Chemical Engineering Department, Chungnam National University ) , Lee Jeewon (Biochemical Process Engineering R.U., Korea Research Institute of Bioscience and Biotechnology (KRIBB) ) , Kim In-Ho (Chemical Engineering Department, Chungnam National University ) , Park Young-Hoon (Biochemical Process Engineering R.U., Korea Research Institute of Bioscience and Biotechnology (KRIBB))
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 13 - 16 , 2000 , 1226-8372 ,

    초록

    Simple procedures have been devised for purifying recombinant human interleukin-2 (hIL-2), which was expressed in Escberichia coli using sequences of glucagon molecules and enterokinase cleavage site as an N-terminus fusion partner. The insoluble aggregates of recombinant fusion protein produced in E. coli cytoplasm were easily dissolved by simple alkaline pH shift $(8\rightarrow12\rightarrow8)$ . Following enterokinase cleavage, the recombinant hIL-2 was finally purified by one-step reversed-phase HPLC with high purity. The ease and high efficiency of this simple purification process seem to mainly result from the role of used glucagon fusion partner, which could be applied to the production of other therapeutically important proteins.

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  5. [국내논문]   Chiral Separation of Tryptophan Enantiomers by Liquid Chromatography with BSA-Silica Stationary Phase  

    Kim Kwonil (Dept. of Environmental Engineering and Biotechnology, Myongji University ) , Lee Kisay (Dept. of Environmental Engineering and Biotechnology, Myongji University)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 17 - 22 , 2000 , 1226-8372 ,

    초록

    The separation of tryptophan enantiomers was carried out with medium-pressure liquid chromatography using BSA (bovine serum albumin)-bonded silica as a chiral stationary phase. The influence of various experimental factors such as pH and ionic strength of mobile phase, separation temperature, and the presence of organic additives on the resolution was studied. In order to expand this system to preparative scale, the loadability of sample and the stability of stationary phase for repeated use were also examined. The separation of tryptophan enantiomers was successful with this system. The data indicated that a higher separation factor (a) was obtained at a higher pH and lower temperature and ionic strength in mobile phase. Addition of organic additives (acetonitrile and 2-propanol) in mobile phase contributed to reduce the retention time of L-tryptophan. About $30\%$ of the separation factor was reduced after 80 days of repeated use.

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  6. [국내논문]   Identification of Genetic Markers for Korean Native Cattle (Hanwoo) by RAPD Analysis   피인용횟수: 1

    Yeo Jung Sou (Department of Animal Sciences, College of Natural Resources, Yeungnam University ) , Lee Ji Sun (Division of Pharmacy, College of Pharmacy, Yeungnam University ) , Lee Chang Hee (Division of Pharmacy, College of Pharmacy, Yeungnam University ) , Jung Young Ja (Korea Food and Drug Administration ) , Nam Doo Hyun (Division of Pharmacy, College of Pharmacy, Yeungnam University)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 23 - 26 , 2000 , 1226-8372 ,

    초록

    In order to develop the specific genetic marker for Korean native cattle (Hanwoo), randomly amplified polymorphic DNA (RAPD) analysis of 6 different cattle breeds was attempted by using 38 decamer primers. In comparison of RAPD patterns, two distinctive DNA bands specific for Hanwoo were detected. One was 296 bp of DNA fragment found to be specific only for female Hanwoo when primer GTCCACACGG was employed. In individual analysis of this RAPD marker was observed only in female individuals with the possibility of $85.3\%$ . The other was 521 bp of RAPD marker amplified using TCGGCGATAG and AGCCAGCGAA primers, which showed $83.0\%$ of genetic frequency in 85 male and 68 female individuals tested. Nucleotide sequencing of these genetic markers revealed that 296 bp marker has a short micro satellite-like sequence, ACCACCACAC, and a tandem repeat sequence of microsatellite GAAAAATG in the determined sequence. Two distinctive tandem repeats of microsatellite sequences, MC and GAAGA, were also appeared in 521 bp DNA marker. In BLAST search, any gene having high homology with these markers was not found.

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  7. [국내논문]   A Parametric Study on Ethanol Production from Xylose by Pichia stipitis  

    Lee Tae-Young (Department of Food Science & Technology and Research Center for New Bio-Materials in Agriculture, Seoul National University ) , Kim Myoung-Dong (Department of Food Science & Technology and Research Center for New Bio-Materials in Agriculture, Seoul National University ) , Kim Kyu-Yong (Department of Food Science & Technology and Research Center for New Bio-Materials in Agriculture, Seoul National University ) , Park Kyungmoon (Ministry of Commerce, Industry and Energy ) , Ryu Yeon-Woo (Department of Molecular Science and Technology, Ajou University ) , Seo Jin-Ho (Department of Food Science & Technology and Research Center for New Bio-Materials in Agriculture, Seoul National University)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 27 - 31 , 2000 , 1226-8372 ,

    초록

    Characteristics of ethanol production by a xylose-fermenting yeast, Pichia stipitis Y-7124, were studied. The sugar consumption rate and specific growth rate were higher in the glucose-containing medium than in the xylose-containing medium. Specific activities of xylose reductase and xylitol dehydrogenase were higher in the medium with xylose than glucose, suggesting their induction by xylose. Maximum specific growth rate and ethanol yield were achieved at 30 g xylose/L concentration without formation of by-products such as xylitol and acetic acid whereas a maximum ethanol concentration was obtained at 130 g/L xylose. Adding a respiratory inhibitor, rotenone, increased a maximum ethanol concentration by $10\%$ compared with the control experiment. In order to evaluate the pattern of ethanol inhibition on specific growth rate, a kinetic model based on Luong's equations was applied. The relationship between ethanol concentration and specific growth rate was hyperbolic for glucose and parabolic for xylose. A maximum ethanol concentration at which cells did not grow was 33.6 g/L for glucose and 44.7 g/L for xylose.

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  8. [국내논문]   Application of a Compatible Xylose Isomerase in Simultaneous Bioconversion of Glucose and Xylose to Ethanol   피인용횟수: 1

    Chandrakant Priya (Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology ) , Bisaria Virendra S. (Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 32 - 39 , 2000 , 1226-8372 ,

    초록

    Simultaneous isomerisation and fermentation (SIF) of xylose and simultaneous isomerisation and cofermentation (SICF) of glucose-xylose mixture was carried out by the yeast Saccharomyces cerevisiae in the presence of a compatible xylose isomerase. The enzyme converted xylose to xylulose and S. cerevisiae fermented xylulose, along with glucose, to ethanol at pH 5.0 and $30^{\circ}C$ . This compatible xylose isomerase from Candida boidinii, having an optimum pH and temperature range of 4.5-5.0 and $30-35^{\circ}C$ respectively, was partially purified and immobilized on an inexpensive, inert and easily available support, hen egg shell. An immobilized xylose isomerase loading of 4.5 IU/(g initial xylose) was optimum for SIF of xylose as well as SICF of glucose-xylose mixture to ethanol by S. cerevisiae. The SICF of 30 g/L glucose and 70 g xylose/L gave an ethanol concentration of 22.3 g/L with yield of 0.36 g/(g sugar consumed) and xylose conversion efficiency of $42.8\%$ .

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  9. [국내논문]   Effect of Zinc on Vascular Smooth Muscle Cell Death Mediated by PDTC  

    Moon Sung-Kwon (Univ. of Texas Medical Branch, Div. of Cardiology and Sealy, Center for Molecular Cardiology ) , Ha Sang-Do (Dept. of Industry and Technology, Korea Health Industry Development Institute)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 40 - 43 , 2000 , 1226-8372 ,

    초록

    Pyrrolidinedithiocarbamate (PDTC) and N-Acetylcysteine (NAC) are metal and nonmetal-chelating antioxidant which can induce rat and human smooth muscle cell death. When the smooth muscle cells from mouse aorta (MASMC) that we successfully cultured recently was exposed to PDTC and NAC in a normal serum state, the cells were induced to death by these compounds. However, PDTC did not induce the cell death in a serum depleted medium. This data suggests that certain factors in the serum may mediate the cytotoxic effect of PDTC. The metal chelator, Ca-EDTA blocked PDTC-induced cell death, but Cu-, Fe-, and Zn-EDTA did not block the PDTC-induced cell death. This data indicated that copper, iron, and zinc in the serum may lead to the cytotoxic effect of PDTC. Investigation of the intracellular zinc level in PDTC-induced smooth muscle cell death using the zinc probe dye N-(6-methoxy-8-quinolyl)-p-toluenesulfonamide shows that only the muscle-containing layers of the arteries have higher level of zinc. As expected, PDTC increased the intracellular fluorescence level of the zinc. In agreement with these results, the addition of an exogenous metal, zinc, induced the vascular aortic smooth muscle cell death which led to an increased intracellular zinc level. We concluded that PDTC induced mouse aortic smooth muscle cell death required not only zinc level but also intracellular copper and iron level. The mechanism of this antioxidant to induce vascular smooth muscle cell death may provide a new strategy to prevent their proliferation in arteriosclerotic lesions.

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  10. [국내논문]   Enhanced Proliferation and Altered Intracellular Zinc Levels in Early- and Late-Passage Mouse Aorta Smooth Muscle Cells  

    Moon Sung-Kwon (Univ. of Texas Medical Branch, Div. of Cardiology and Sealy, Center for Molecular Cardiology ) , Ha Sang-Do (Dept. of Industry and Technology, Korea Health Industry Development Institute)
    Biotechnology and bioprocess engineering v.5 no.1 ,pp. 44 - 47 , 2000 , 1226-8372 ,

    초록

    Cell growth and DNA synthesis were studied from a cultured early- and late- pas- sage mouse aorta smooth muscle cell (MASMC) because the proliferation of vascular smooth muscle cell (VSMC) is a key factor in development of atherosclerosis. In this study, the cells were cultured in fetal bovine serum (FBS) and stimulated by growth factors such as thrombin and platelet-derived growth factor-BB (PDGF-BB). Compared to the number of early-passage MASMC (passage 3 to 9) the number of late-passage MASMC (passage 30 to 40) in a normal serum state was increased 2 fold at Day 1, 3 and 6 in culture, respectively. Incorporation of $[^3H]$ thymidine into DNA induced by serum, PDGF and thrombin in late-passage MASMC was greater than those in early-passage MASMC. We also examined whether intracellular zinc levels would be an aging factor or not. The intracellular zinc level in early- and late-passage MASMC was monitored by using the zinc probe dye N-(6-methoxy-8-quinolyl)-p-toluenesulfonamide. It is interested that late-passage MASMC increased the intracellular fluorescence level of zinc, more than the early passage MASMC did. The alterations of intracellular zinc level occur concurrently with changes in MASMC proliferation rate during aging. This data suggest that the age-associated changes in zinc concentrations may provide a new in vitro model for the study of smooth muscle cell differentiation.

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