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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 85-92 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glucoamylase bound to DEAE-cellulose in 0.05 M sodium acetate, pH 4.0, is active in the conversion of starch to glucose. The activity of the DEAE-cellulose-bound enzyme ranges from 16 to 55% of the activity of the free enzyme. Binding of the enzyme narrows the pH optimum to approximately 4.0 and lowers the temperature optimum to 40-50°C as compared to a 60°C temperature optimum for the free enzyme. Concentrations of acetate buffer above 0.1 M disrupt the DEAE-cellulose-enzyme complex. Columns were used with some success for the continuous conversion of starch. Pretreatment of the starch with α-amylase and clarification were necessary to prevent blocking of the column. Columns maintained activity for more than 3 weeks of continuous operation.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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