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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 313-319 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A comparative study of the Bacillus subtilis neutral protease and Bacillus thermoproteolyticus thermolysin calalyzed hydrolysis of a few dipeptide sustrates including furylacryloylglycyl-L-leucine amide is reported. While differences in the kcat/Km were observed between the two enzymes toward substrates in which phenylalanine or leucine donated the amino group of the peptide bond, secondary effects of substituents on the carbonyl donating amino acid and pH profiles were quite similar. Differences were also observed toward protein substrates as compared to dipeptides.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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