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  • Schwanniomyces castellii  (4)
  • chemostat culture  (2)
  • Amylase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Influence of culture conditions on the cell yield and amylases biosynthesis in continuous culture by Schwanniomyces castellii (1987)
    Springer
    Archives of microbiology 148 (1987), S. 162-166 
    Details
    ISSN: 1432-072X
    Keywords: Schwanniomyces castellii ; Amylase ; Continuous culture ; Starch ; Cell yield
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Schwanniomyces castellii excreted α-amylase and amyloglucosidase into the medium in the presence of starch. The biosynthesis and the rate of excretion were influenced by dissolved oxygen (specially for α-amylase), pH of the culture and dilution rate. The cell yield observed (0.59) remained constant up to D=0.35h-1 with starch as substrate. But in the case of growth on glucose, the yield observed was equal to 0.62 up to a dilution rate of D=0.18 h-1. Beyond this value Y x/s decreased and ethanol was produced. The onset of fermentation dependend partly on the nature of the substrate and not only on the environment in particular on the quantity of dissolved oxygen present.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425367
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Alternative respiration pathways in Schwanniomyces castellii (1990)
    Springer
    Antonie van Leeuwenhoek 57 (1990), S. 131-137 
    Details
    ISSN: 1572-9699
    Keywords: Schwanniomyces castellii ; oxidation pathways
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By using cytochrome-deficient mutants of Schwanniomyces castellii found previously, we measured the inhibition constants of azide and SHAM—alone or combined—for the different oxidative pathways, in order to determine the more suitable concentrations of inhibitors. This allowed us to measure the real capacity of each pathway. We calculated their affinity for oxygen, and determined that O2 was preferencially reduced by the cytochromic pathway, then by the SHAM-sensitive pathway, and finally by the SHAM+AA-insensitive pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403947
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Alternative respiration pathways in Schwanniomyces castellii (1990)
    Springer
    Antonie van Leeuwenhoek 57 (1990), S. 123-130 
    Details
    ISSN: 1572-9699
    Keywords: Schwanniomyces castellii ; alternative respiration ; cytochrome-deficient
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated and studied cytochromic-deficient mutants of the amylolytic yeast Schwanniomyces castellii in order to study the possible contribution of cytochromes to alternative pathways. Three mutants were found, lacking cytochrome b, a+a 3,or b and a+a 3.All strains presented two alternative pathways, which were induced in the wild strain when cytochromic respiration was suppressed by growth in the presence of inhibitors, or without copper. If cytochromic respiration was absent, the $${\text{Y}}_{_{\bar S}^x } $$ yields in aerobiosis were higher than in anaerobiosis. This shows that the alternative pathways play a part in energy conservation. Cytochrome chrome a+a 3did not appear to be directly involved in the alternative pathways.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403946
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Glucose metabolism, enzymic analysis and product formation in chemostat culture of Hanseniaspora uvarum (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 327-336 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; Hanseniaspora uvarum ; respiration ; fermentation ; chemostat culture ; glucose metabolism ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The physiology of Hanseniaspora uvarum K5 was studied in glucose-limited chemostat cultures and upon glucose pulse. Up to a dilution rate of 0·28 h-1, glucose was completely metabolized in biomass and CO2. Above this value, increase in the dilution rate was accompanied by sequential production of metabolites (glycerol, acetate and ethanol) and decrease in cell yield. Similar results were observed upon glucose pulse. From the enzyme activities (pyruvate dehydrogenase, pyruvate decarboxylase, NAD and NADP-dependent acetaldehyde dehydrogenases, acetyl coenzyme A synthetase and alcohol dehydrogenase) and substrate affinities, the following conclusions were drawn with respect to product formation of cells: (1) pyruvate was preferentially metabolized via pyruvate dehydrogenase, when biomass and CO2 were the only products formed; (2) acetaldehyde formed by pyruvate decarboxylase was preferentially oxidized in acetate by NADP-dependent aldehyde dehydrogenase; acetate accumulation results from insufficient activity of acetyl-CoA synthetase required for the complete oxidation of acetate; (3) acetaldehyde was oxidized in ethanol by alcohol dehydrogenase, in addition to acetate production.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110405
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a hexokinase mutant of Schwanniomyces castellii: Consequences on cell production in continuous culture (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 5 (1989), S. 469-476 
    Details
    ISSN: 0749-503X
    Keywords: Schwanniomyces castellii ; hexokinase ; continuous culture ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A mutant of Schwanniomyces castellii with reduced glucose phosphorylation and with practically no phosphorylation of fructose was investigated. Carbon catabolite represion of α-glucosidase and amylases was reduced. Repression of β-galactosidase was normal. We have compared in continuous culture this mutant strain with wild type and another previously described mutant. The relationship between the specific rate of glucose consumption (Qs) and residual glucose concentration (s) in an inverse mode, suggests that there may be two types of transport of glucose. Mutation at the phosphorylation level causes apparent modification of the kinetic parameters of glucose uptake rate. The consequence of mutation at the phosphorylation level on biomass production was discussed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320050606
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Physiological approach to heterologous human serum albumin production by Kluyveromyces lactis in chemostat culture (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1297-1303 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; Kluyveromyces lactis ; recombinant ; phosphoglycerate kinase ; glycolysis ; heterologous protein ; rHSA ; chemostat culture ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Production of recombinant human serum albumin (rHSA) controlled by the constitutive promoter phosphoglycerate kinase was studied in Kluyveromyces lactis. It was governed by both cell concentration and glycolytic flow. The triggering of the fermentation metabolism by unfavourable culture conditions (pH, pO2, D) caused a decrease in the synthesis of the heterologous protein. The highest productivity (75 mg 1-1 per h) and rHSA concentration (62 mg 1-1) were obtained in chemostat culture with a dilution rate of 0·12 h-1 and with 38 g 1-1 dry weight.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320101006
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    Paper (German National Licenses)
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