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  • 1
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 9 (1989), S. 191-195 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Three cellulase components and one xylanase of Trichoderma sp. M-17 have been immobilzed on a soluble high molecular weight polymer (PVA), using carbodiimide. The immobilized enzymes retained about 80% of the cellulase, cellulose 1,4-β-cellobiosidase, β-glucosidase and 60% endo-1,4-β-xylanase activities. The bound enzymes catalyzed the hydrolysis of alkali-treated cornstalks with a higher efficiency than the free cellulase. The potential for reutilization of the immobilized enzymes was studied using membrane filters and the system was found to be active for three cycles.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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