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  • 1
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 13 (1993), S. 21-30 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pretreated wheat straw was enzymatically hydrolyzed in 250-ml flasks using the culture filtrate of Trichoderma reesei QM-9414. The influence of the initial enzymatic activity in the liquid phase was studied. The unreacted core model was used to analyze the experimental data obtained at 40, 46 and 50°C. The model adequately describes the data for hydrolysis times lower than 10 h.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 12 (1992), S. 357-364 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cellulase from four different fungi and β-glucosidase from almonds were immobilized on the inner surface of nylon tubing. The highest values of β-glucosidase activity retention on the support were obtained when P. funiculosum and N. crassa were used as the enzyme source. A comparative study of the thermal stability referring to β-glucosidase activity was developed using free and immobilized enzymes. The most stable β-glucosidases (from P. funiculosum and A. niger) did not show an appreciable change in its thermal stability after immobilization. An important increase in thermal stability was observed when less stable β-glucosidases (from T. reesei, N. crassa and almonds) were immobilized.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 19 (1999), S. 3-16 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The kinetics of cellobiose hydrolysis was studied using β-glucosidase from Penicillium funiculosum, both free and immobilized on nylon powder, at different temperatures, pH values, enzymatic activities and initial cellobiose and glucose concentrations.The experimental results were fitted to a kinetic model by considering the substrate and product inhibitions as well as the thermal deactivation of β-glucosidase with a mean deviation of less than 10%. The immobilization of β-glucosidase led to an increase in the stability of the enzyme against changes in the pH value.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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