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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 259 (1976), S. 670-671 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] S. carlsbergensis was grown, collected and assayed for oscillatory metabolism as described before7. The results of one experiment are shown in Fig. 1; Fig. la records, for a period of 8 min in an oxygenated 0.0125% (w/w) yeast suspension, the total culture fluorescence, which correlates with the ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 345-355 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The location of the β-glucosidase activity in a whole culture broth of the thermophilic organism Thermoactinomyces has been studied. Little β-glucosidase activity was found in the culture filtrate, while the culture solids contained the major part of the activity of the whole culture broth. The activity does not appear to be adsorbed to the culture solids; rather there is evidence that it is an intracellular soluble enzyme(s). The pH and temperature optima for a crude β-glucosidase preparation were determined to be pH 6.5 and 50-55°C. Enzyme activity studies indicate that the same enzyme(s) accounts for the β-glucosidase and the cellobiase activities. The validity of using the filter paper activity of culture filtrates from Thermoactinomyces to predict the total saccharification of cellulosic materials to glucose is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A saccharification of cellulosic material using culture filtrate from the stationary phase of a culture of Thermomonospora sp. produced primarily cellobiose up to levels inhibitory to further saccharification, while the use of whole broth resulted in the production of glucose as well. Glucose production was enhanced and continued throughout the saccharification (24-36 hr) by several additions of cellobiase activity in the form of culture solids. Using Solka-Floc as substrate, the “difference sugar” level (total soluble sugar minus glucose) rapidly rose to the same relatively stable concentration under various hydrolysis conditions, which was independent of the total sugar and glucose concentrations. A rapid hydrolusis rate was observed initially during saccharification, followed by a much slower rate of sugar production. Repeated centrifugation of the reaction mixture and replacement of the supernatant with fresh enzyme solution resulted each time in the reinitiation of a rapid hydrolysis rate. Saccharifications using A vicel microcrystalline cellulose, acid-swollen cellulose, and cotton as substrates were also studied. A modified method of making phosphoric-acid swollen cellulose is described. Saccharification of this substrate by culture filtrate and sequential additions of culture solids resulted in an inverse relationship between the attained glucose concentration and cellobiose-cellotriose concentrations.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The stabilities and optima with respect to temperature and pH of the β-glucosidase, Avicelase, and carboxymethylcellulase (CMCase) activity of Thermomonospora sp., in the culture filtrate, culture whole broth, and filtrate after sonication of culture solids, are reported. The β-glucosidase is cell associated and has an optimal activity at about pH 6.5 and 55°C. In the whole culture broth, it has a half-life of about 8 hr at 55°C and less than 1 hr at 60°C, while the half-life of the activity in the sonicated, cell-free filtrate is less than 1 hr at 55°C. The Avicelase and CMCase activities occur in the extracellular culture fluid and have optima at about pH 7.0 and 5.9, and 65 and 70°C, respectively. The CMCase activity is stable over 24 hr at 60°C, but declines by 50% in the same period at 65°C. The Avicelase activity declines by 15% over 24 hr at 55°C, and by 50% at 60°C. The highest pH studied (pH 7.3) was the most destabilizing for all three activities. The thermostable characteristics of the cellulases from Themomonospora appear to make them suitable for commercial saccharification processes operating at elevated temperatures.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 2855-2864 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The cell-associated β-glucosidase activity of Thermomonospora fusca, strain YX, showed both PNPGase and cellobiase activities. The cellobiase activity was found by HPLC assay to have very low product inhibition, whereas the PNPGase activity was more significantly inhibited. Of the various sugars and sugar analogs tested for inhibition of the PNPGase activity, gluconolactone had the greatest effect. The low product inhibition of the cellobiase activity was further demonstrated by the production of glucose syrups to 20% concentration from both cellobiose and swollen cellulose (Avicel). This characteristic is of practical importance in the development of a commercial process for the production of glucose syrups from cellulose. Growth experiments gave further evidence for the probability of separate enzymes for the PNPGase and cellobiase activities.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 2865-2872 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The saccharification of cellulosic substrates by cellulase from Thermomonospora fusca, strain YX, was influenced by the presence of various substances. Cellobiose was strongly inhibitory, reducing the activity against swollen cellulose to 25% at 5% concentration. Glucose had much less effect, reducing activity to 40% at 20% concentration. Ethanol was found to be only slightly inhibitory to the cellulase, reducing activity by about 15% at 6% concentration, but much more inhibitory to the cell-bound β-glucosidase activity. Of the numerous metal ions examined, Ca2+ and Co2+ at 0.1mM-1.0mM concentration were found to be slightly activating under assay conditions, while 1.0mM Pb2+ and Hg2+ were the most inhibitory ions. The implications of these results for the design of commercial processes for ethanol production from cellulose are discussed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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