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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Biotechnology letters 14 (1992), S. 1041-1044 
    ISSN: 1573-6776
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary The influence of pH, temperature, substrate concentration and organic solvents (dimethylformamide, dimethylsulfoxide) on the α-chymotrypsin stability in a water/organic solvent system was studied. The enzyme activity was measured as the dipeptide, AcPheLeuNH2 synthesis and the ester substrate hydrolysis. Enzyme stability was enhanced by lower pH and temperature values and higher substrate concentrations. Dimethylsulfoxide allowed an higher enzyme stability than dimethylformamide. α-Chymotrypsin displayed an higher stability in the water medium when it was compared to the organic system.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 1031-1042 
    ISSN: 0006-3592
    Schlagwort(e): peptide synthesis ; alcohol ; chemical modification ; α-chymotrypsin ; reverse micelles ; response ; surface methodology ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: The influence of the long chain alcohols, hexanol, octanol, and decanol, as cosurfactants of the reverse micellar system of tetradecyltrimethylammonium bromide on the α-chymotrypsin-mediated AcPheLeuNH2 synthesis was studied. The effect of temperature, buffer molarity, pH, and substrate concentration was also evaluated. The enzyme was chemically modified and the effect of this modification upon the enzyme activity was also analyzed. Octanol allowed a higher activity for both enzyme forms. The peptide synthesis/substrate hydrolysis ratio is independent of the long chain alcohol used. The chemical modification decreases the α-chymotrypsin activity under the system conditions studied, but increases the initial velocity of peptide synthesis relative to the ester substrate hydrolysis. The response surface methodology was applied to optimize the dipeptide synthesis in the system containing octanol as cosurfactant. © 1994 John Wiley & Sons, Inc.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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