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  • 1
    Electronic Resource
    Electronic Resource
    Antimicrobial Effect of Pressurized Carbon Dioxide on Listeria monocytogenes (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 59 (1994), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Listeria monocytogenes was inactivated by carbon dioxide at 35 and 45°C under pressures of 70.3 and 210.9 μg/cm2. Inactivation rates were sensitive to temperature and pressure. Other factors such as pH, moisture content, and environmental conditions of cell growth also influenced the effectiveness of CO2 treatment. Bacteria were more difficult to inactivate when they were suspended in the medium with fat or oil, which may have protected the cells from penetration by CO2. Fat in growth medium where Listeria monocytogenes cells were inoculated apparantly increased their resistance. Several methods may be useful for increasing inactivation rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb05587.x
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  • 2
    Electronic Resource
    Electronic Resource
    Fermentation of Sugarcane Bagasse Hemicellulose Hydrolysate to Xylitol by a Hydrolysate-Acclimatized Yeast (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The yeast strain, Candida sp B-22, which has an increased tolerance to untreated neutralized sugarcane bagasse hemicellulose hydrolysate has been isolated by a continuous adaptation-selection technique which allows yeasts to overcome the inhibitory effect of extraneous chemicals in hydrolysate. With this yeast, xylitol is produced from untreated full-strength hydrolysate in a yield of over 85% of the theoretical value. A final xylitol concentration of 94.74 g/L was obtained from 105.35 g/L D-xylose in hemicellulose hydrolysate after 96 hr of incubation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13315.x
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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Effect of inoculum on yeast cell aggregation (1986)
    Springer
    Applied microbiology and biotechnology 25 (1986), S. 232-237 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Saccharomyces uvarum, Kluyveromyces marxianus, Saccharomyces cerevisiae, and Candida sp. were induced to form cell aggregates in a column. The conditions for this induction were high cell density and slow flow rate; with K. marxianus and Candida sp., the presence of ethanol in the growth medium was also required. When these aggregated cells were inoculated into a fresh growth medium, the ability of the progeny cells to aggregate depended on the state of the inoculum. If the aggregates were not disrupted, the progeny cells remained as aggregates, and if the aggregates were dispersed by vortexing before inoculation, the progeny cells because a free cell suspension.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253655
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  • 5
    Electronic Resource
    Electronic Resource
    Production, separation and purification of yeast invertase as a by-product of continuous ethanol fermentation (1991)
    Springer
    Applied microbiology and biotechnology 36 (1991), S. 44-47 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A strain of Saccharomyces uvarum produced extracellular invertase in a chemostat reactor using a medium containing corn steep liquor and sugars. The production of yeast invertase increased with increase in corn steep liquor concentration. The production rate of invertase was maximal at a dilution rate of 0.75 h−1. The production rate of invertase was found to be affected by the type of sugar substrate and fermentation temperature. The invertase in the crude broth could be purified by one-step DEAE chromatography. An 84% enzyme recovery with ninefold purification and 30-fold concentration could be achieved using this simple isolation procedure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00164697
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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Physical characteristics of porous cellulose beads as supporting material for immobilized enzymes (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1507-1516 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cellulose beads prepared in this report have high porosity (75-80%) and evenly distributed pores. The pore size is about 1000 Å. The cellulose beads are physically strong and contain large amounts of reactive groups, making them suitable for use as carriers for immobilized enzymes.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181103
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  • 8
    Electronic Resource
    Electronic Resource
    Characteristics of yeast invertase immobilized on porous cellulose beads (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 365-375 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Invertase from Candida utilis was immobilized on porous cellulose beads by an ionic-quanidino bond. The immobilized invertase showed optimum activity between pH 4.0 and 5.4, while the free enzyme had a sharp optimum at pH 4.1. Both temperature profiles were fairly similar up to 55°C. However, above this temperature the immobilized enzyme was more stable than the free enzyme. From the temperature data, the activation energies were found to be 7,322 and 4,052 cal/g mol for the free and the immobilized enzyme, respectively.Candida invertase shows characteristics of substrate inhibition. Both the Km and Ki for the free and the immobilized enzymes were determined. The apparent Ki for the immobilized invertase was much higher than the Ki of the free enzyme, suggesting a diffusion effect. Immobilized invertase molecules deep in the pores only see sucrose concentrations much less than the bulk concentrations. Immobilization, thus, offers certain processing advantages in this regard.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260190307
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  • 9
    Electronic Resource
    Electronic Resource
    Chemical procedures for enzyme immobilization on porous cellulose beads (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 1463-1473 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In a previous article, the method of preparation and the physical properties of porous (75 to 80% porosity) cellulose beads were described (Biotechnol. Bioeng., 18, 1057 (1976)). The present article reports that the chemical procedures employed for immobilizing enzymes on ordinary cellulose can be applied to the porous cellulose beads. The results showed more enzyme loading on the beads than ordinary cellulose. The choice of the procedures might also affect the mechanical strength of the cellulose beads.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260191005
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  • 10
    Electronic Resource
    Electronic Resource
    Preparation of immobilized soybean β-amylase on porous cellulose beads and continuous maltose production (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 383-402 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized soybean β-amylase was prepared by using porous cellulose beads. The expressed activity of the β-amylase-cellulose beads conjugated below 35 mesh was 59-69% of the initial activity and the protein content was 10-13%. General properties of the conjugate were almost identical with those of the native enzyme except for the Km value. The Km value of the conjugate was 40mM and the Km value of the native enzyme was 0.6mM. This large difference was probably caused by pore structure, i.e., a pore diffusion problem. The film diffusion problem occurred at the flow rate below a linear velocity of 3 cm/min. Maximum maltose contents of the hydrolyzates prepared by the conjugate and the native enzyme were 69 and 71%, respectively. After a continuous column operation at 50°C for 17 days, the activity of the column was 60% of the activity. The half-life of the column at 40°C was 40 days.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260200305
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