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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 254-257 
    ISSN: 0006-3592
    Keywords: oxalate oxidase ; PEG-immobilized oxalate oxidase ; polyethylene glycol ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Oxalate oxidase (EC 1.2.3.4), obtained from the beet stem, was covalently linked to polyethylene glycol (PEG). Compared with native enzyme, the modified oxalate oxidase exhibited decreased electrophoretic mobility, increased storage stability, higher thermal stability, and resistance to heavy metal inactivation and proteolytic digestion. The chemical modification of oxalate oxidase with PEG also brought about a marked shift in its optimal pH, from pH 4.5 to 6.5, without altering its Michaelis constant (Km) significantly. These acquired properties of the immobilized oxalate oxidase render it suitable for possible applications in clinical, nutritional, and medical fields. © 1995 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1611-1614 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A simple procedure for the entrapment of enzymes in nylon-reinforced cellulose triacetate fibers and the fabrication of reusable enzyme brushes using such fiber bristles for the analytical determination of unknown samples have been described. As an example, enzyme brushes of lactate dehydrogenase were fabricated and were repeatedly employed for the determination of pyruvic acid in clinical samples in place of soluble enzymes. The above brush method compared well with that of wet enzymic analysis of pyruvate in clinical samples in accuracy, sensitivity, and reproducibility. The device also proved to be easy to handle, use, and reprocess for repeated analyses.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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