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  • Articles  (3)
  • Saccharomyces cerevisiae
  • yeast
  • 2000-2004  (3)
  • Process Engineering, Biotechnology, Nutrition Technology  (3)
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  • Articles  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    A novel method for immobilization of invertase from the thermophilic fungus, Thermomyces lanuginosus (2000)
    Springer
    World journal of microbiology and biotechnology 16 (2000), S. 151-154 
    Details
    ISSN: 1573-0972
    Keywords: Invertases ; immobilization ; phenyl-Sepharose ; thermophilic fungus ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An invertase from the thermophilic fungus, Thermomyces lanuginosus was immobilized on phenyl-Sepharose and its properties were studied. Between the soluble and immobilized forms of the invertase, there were not much difference in their optimum pH, K M and V max for sucrose. In contrast, the K M and V max for raffinose changed significantly. The optimum temperature for the immobilized invertase was lower by 10 ∘C. The immobilized invertase showed remarkable stability at 50 ∘C and was less sensitive to inhibition by metal ions. There was no leaching of the enzyme for at least a month when stored in the refrigerator. The method is novel and specific for the thermophilic invertase as a mesophilic invertase (from yeast) did not bind to phenyl-Sepharose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008901801373
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  • 2
    Electronic Resource
    Electronic Resource
    Evaluation of the maximum specific growth rate of a yeast indicating non-linear growth trends in batch culture (2000)
    Springer
    World journal of microbiology and biotechnology 16 (2000), S. 613-616 
    Details
    ISSN: 1573-0972
    Keywords: Absolute error ; specific growth rate ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The maximum specific growth rate (μmax) of an ethanolic D-xylose-fermenting yeast, Pichia stipitis, showing non-linear growth trends in batch culture, was calculated using the rate equation μ2 = (1/Δt) ln(x 2/x 1). The absolute error Δμ, affecting μ2, was derived using an equation given by Borzani (1994). Based on the assumption of linearity of growth curves between two closest time points, the relation between the two rate formulae, μ1 = (1/x¯)dx t /dt and μ2 = (1/Δt) ln(x 2/x 1) was established. In a particular condition, when μ1 = μ2, an equation has been developed, the roots of which are the specific growth rates at different time points.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008980317225
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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical characterization of neutral trehalase activity in Saccharomyces boulardii (2000)
    Springer
    World journal of microbiology and biotechnology 16 (2000), S. 691-694 
    Details
    ISSN: 1573-0972
    Keywords: Neutral trehalase ; Saccharomyces boulardii ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Lyophilized cells of the non-pathogenic yeast Saccharomyces boulardii are used in many countries for the treatment of several types of diarrhoea and other gastrointestinal diseases. Although the cells must be viable, their mechanism of action is unknown. The disaccharide trehalose is a protectant against several forms of environmental stress in yeast and is involved in maintaining cell viability. There is no information on the enzymes involved in degradation of trehalose in S. boulardii. The aim of the present study was to characterize trehalase activity in this yeast. Cells of S. boulardii grown in glucose exhibited neutral trehalase activity only in the exponential phase. Acidic trehalase was not detected in glucose medium. Cells grown in trehalose exhibited acid and neutral trehalase activities at all growth stages, particularly in the exponential phase. The optimum pH and temperature values for neutral trehalase activity were determined as 6.5 and 30 °C respectively, the half-life being approximately 3 min at 45 °C. The relative molecular mass of neutral trehalase is 80 kDa and the K m 6.4 mM (±0.6). Neutral trehalase activity at pH 6.5 was weakly inhibited by 5 mM EDTA and strongly inhibited by ATP, as well as the divalent ions Cu++, Fe++ and Zn++. Enzyme activity was stimulated by Mg++ and Ca++ only in the absence of cAMP. The presence of cAMP with no ion additions increased activity by 40%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008966501012
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