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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biotechnology letters 21 (1999), S. 595-599 
    ISSN: 1573-6776
    Keywords: α-chymotrypsin ; enzyme stability ; glycosylated enzymes ; kyotorphin ; peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract α-Chymotrypsin was covalently modified with cellobiose by chemical means. After adsorption on to a porous polyamide support, both the native and the glycosylated immobilized derivatives were used to synthesize a kyotorphin derivative (N-benzoyl-l-tyrosyl-l-argininamide) in acetonitrile/water. Glycosylated chymotrypsin gave a 125% increase in product formation (750 nmol mg−1 catalyst in 3 h) at 60% (v/v) acetonitrile/water. Maximal protective effect of this glycosylation process was at 70% (v/v) acetonitrile/water, at which concentration the half-life of the glycosylated enzyme was 20-times longer than that of the native form (52 min and 2.8 min, respectively).
    Type of Medium: Electronic Resource
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