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  • 1
    Electronic Resource
    Electronic Resource
    Disintegration of yeast cells by pressurized carbon dioxide (1991)
    s.l. : American Chemical Society
    Biotechnology progress 7 (1991), S. 201-204 
    Details
    ISSN: 1520-6033
    Source: ACS Legacy Archives
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bp00009a001
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  • 2
    Electronic Resource
    Electronic Resource
    Integration and expression of theEscherichia coli xylose isomerase gene inSchizosaccharomyces pombe (1989)
    Springer
    Journal of industrial microbiology and biotechnology 4 (1989), S. 409-417 
    Details
    ISSN: 1476-5535
    Keywords: Schizosaccharomyces pombe ; Xylose isomerase gene ; Xylose fermentation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The xyclose isomerase gene inEscherichia coli was cloned complementarily into a Leu2-negativeSchizosaccharomyces pombe mutant (ATCC 38399). The subsequent integration of the plasmid into the chromosomal DNA of the host yeast was verified by using the dot blot and southern blot techniques. The expressed xylose isomerase showed activity on a nondenaturing polyacrylamide gel. The expression of xylose isomerase gene was influenced by the concentration of nutrients in the fermentation broth. The yeast possessed a xylose isomerase activity of 20 nmol/min/mg by growing in an enriched medium containing yeast extract-malt extract-peptone (YMP) andd-xylose. The conversion ofd-xylose tod-xylulose catalyzed by xylose isomerase in the transformed yeast cells makes it possible to fermentd-xylose with ethanol as a major product. When the fermentation broth contained YMP and 5% (w/v)d-xylose, the maximal ethanol yield and productivity reached 0.42 g/g and 0.19 g/l/h, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569636
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  • 3
    Electronic Resource
    Electronic Resource
    Stimulation of n-alkane conversion to dicarboxylic acid by organic-solvent- and detergent-treated microbes (1991)
    Springer
    Applied microbiology and biotechnology 34 (1991), S. 772-777 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A wild-type strain of Cryptococcus neoformans and Pseudomonas aeruginosa were used to convert n-pentadecane to the corresponding dioic acid, tridecane 1,13-dicarboxylic acid (DC-15). Altering the cell permeability by treating C. neoformans with 1% (v/v) toluene or 7% (v/v) Triton X-100 stimulated production of DC-15 by 1.5-fold and fourfold, respectively. Furthermore, DC-15 productivity was increased from 2.5 mg/l per hour to 18 or 30 mg/l per hour, respectively. If 10% (v/v) hexane was used to treat the yeast culture, stimulation of DC-15 production could reach 200% and more viable cells remained compared to the toluene-treated culture. Data from the organic solvent treatment experiment indicated that the solvent with a higher polarity showed a more adverse effect on DC-15 production. P. aeruginosa was vulnerable to most organic solvents; however, Tween 80 could greatly stimulate the conversion of n-pentadecane to DC-15. Although organic solvents and non-ionic detergents could enhance DC-15 formation by microbial conversion, it was inhibited by elevated levels of DC-15.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169348
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  • 4
    Electronic Resource
    Electronic Resource
    Metabolism of d-xylose in Schizosaccharomyces pombe cloned with a xylose isomerase gene (1989)
    Springer
    Applied microbiology and biotechnology 31 (1989), S. 524-528 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The Escherichia coli xylose isomerase gene was transformed into Schizosaccharomyces pombe for direct d-xylose utilization. In order to understand d-xylose metabolism and determine the limiting factors on d-xylose utilization by the transformed yeast, d-xylose transport, xylose isomerization, and xylulose phosphorylation were investigated. The results indicated that low activity of xylose isomerization in the cloned yeast was the limiting step for d-xylose fermentation. An in vitro study showed that yeast proteases decreased xylose isomerase activity. Xylitol, a by-product of d-xylose fermentation, had no effect on the activity of xylose isomerase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270788
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  • 5
    Electronic Resource
    Electronic Resource
    Amplification of the tryptophan operon gene in Escherichia coli chromosome to increase l-tryptophan biosynthesis (1993)
    Springer
    Applied microbiology and biotechnology 40 (1993), S. 301-305 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Classical mutagenesis could desensitize the feedback inhibition of l-tryptophan (l-Trp) biosynthesis. Among the mutants, a5-fluorotryptophan-resistant strain, Escherichia coli EMS4-C25 produced 3 g/l of l-Trp within 18 h. The feedback-resistant l-Trp operon gene (trp) prepared from E. coli EMS4-C25 was inserted into pUC19 and pHSG576 to generate pTC701 and pTC576, respectively. When pHSG576 and pTC701 were introduced into E. coli EMS4-C25, chromosomal integration occured through homologous recombination. By using Souther hybridization, we demostrated that the integrated plasmids existed as multicopies. The strains with integrated foreign trp operon gene had higher activities of anthranilate synthase and Trp synthase than those found for the host strain and produced 9.2 g/l of l-Trp with 13% conversion yield from d-glucose. The integration and implification of the trp-operon-beraing plasmid avoided the plasmid instability and increased l-TRp production.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170384
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  • 6
    Electronic Resource
    Electronic Resource
    D-Xylose fermentation to ethanol bySchizosaccharomyces pombe cloned with xylose isomerase gene (1986)
    Springer
    Biotechnology letters 8 (1986), S. 231-234 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Schizosaccharomyces pombe cloned with the xylose isomerase gene from E. coli is able to grow on YNB and YMP broths containing xylose as the sole carbon source. This yeast can ferment D-xylose to ethanol directly; however, the ethanol production rate and the yield were dependent on the nitrogen source. With the YMP broth as a nitrogen source, the final ethanol concentration can reach 3.7% (w/v), and the ethanol yield was 80% of the theoretical value based on the amount of xylose that was metabolized. The ethanol production is slow, and the xylitol production is still very active; apparently, the limiting step is the isomerization of xylose to xylulose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01030503
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  • 7
    Electronic Resource
    Electronic Resource
    Recovery of yeast invertase from ethanol fermentation broth (1992)
    Springer
    Biotechnology letters 14 (1992), S. 573-576 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Ethanol fermentation broth produced by an aggregated form ofSaccharomyces uvarum strain contained invertase when sucrose-based raw materials were used. The amount of invertase in the borth was in the range of 1.4 to 4.8 units/ml, which was affected by the dilution rate, the concentration of corn steep liquor, and the type of sugar used. The activity of invertase in the broth could be maintained at 0.8 units/ml over two months. When the broth was passed through DEAE-cellulose beads and eluted with a NaCl-Tris-HCl buffer solution, a 75% recovery yield of invertase with 9-fold purification and 30-fold concentration could be achieved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01023943
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  • 8
    Electronic Resource
    Electronic Resource
    Effects of recombinant lysostaphin on cytotoxicity and interleukin-8 level in normal human epidermal keratinocytes cell line (1998)
    Springer
    Biotechnology letters 20 (1998), S. 1053-1056 
    Details
    ISSN: 1573-6776
    Keywords: recombinant lysostaphin ; cytotoxicity ; interleukin-8
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The normal human epidermal keratinocyte (NHEK) was used to evaluate the cytotoxicity of recombinant lysostaphin. As determined with the Neutral Red (NR) cytotoxicity assay, the midpoint toxicity value (NR50) after 48 h exposure was 16 ± 0.4 g lysostaphin/l. Lysostaphin cytotoxicity effect is much less than the surface active agent, sodium laurate. However, the NR50 value after 48-h exposure was 1.9 ± 0.02 g/l for S. aureus lysate derived from the bacterial lytic action of lysostaphin. A linear increase in interleukin-8 (IL-8) level in NHEK cells from resting levels of 65 ± 3 pg/ml to peak of 760 ± 15 pg/ml during the first 9 hours was noted for the cells treated with 800 mg lysostaphin/l. S. aureus lysate has the same effect on the induction of IL-8 levels. The induced rises in IL-8 were lysostaphin and S. aureus lysate concentration dependence. © Rapid Science Ltd. 1998
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005469929961
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  • 9
    Electronic Resource
    Electronic Resource
    A synthetic complement C1q-like peptide selectively interacts with immune complexes (1998)
    Springer
    Biotechnology letters 20 (1998), S. 1119-1123 
    Details
    ISSN: 1573-6776
    Keywords: human complement C1q-like peptide ; immune complex ; hydrophilicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A water-soluble peptide possessing an immune complex selective affinity was synthesized and its primary structure established as: Leu-Glu-Gln-Gly-Glu-Asn-Val-Phe-Leu-Gln-Ala-Thr-Ser-Asp-Asp-Cys. This peptide, designated as C1q-like peptide (CLP), represents a possible immune complex binding epitope of complement C1q. CLP has a hydrophilicity value of 0.21. At 0.5 μM, it inhibited by 50% natural human C1q from binding to horseradish peroxidase-rabbit anti-peroxidase immune complex. CLP failed to inhibit Staphylococcus aureus protein A from binding monomeric IgG. When coated to a microplate, CLP showed selective binding to the immune complex, and could be used for application in immunochemical detection of immune complex. © Rapid Science Ltd. 1998
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005368118207
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning a mutatedtrp operon for the biosynthesis of an antibiotic agent (1994)
    Springer
    Biotechnology letters 16 (1994), S. 1021-1026 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Plasmid pCG8 containing a mutatedtrp operon was constructed and introduced into anEscherichia coli host for increasing tryptophan biosynthesis. Since tryptophan is a biosynthetic precursor of pyrrolnitrin, the mutated trp operon was inserted into aPseusdomonas vector pME290 to obtain the plasmid pCG12, and then was introduced intoPseudomonas pyrrocinia for enhancing the pyrrolnitrin synthesis. Data showed that the production of pyrrolnitrin of the transformed strain was five-times greater than that of the parental strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01022396
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