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Pptidase activities in group N streptococci.

J J Sullivan, G R Jago, L Mou

    The Journal of Dairy Research
    |February 1, 1975
    PubMed
    Summary

    This study identified and characterized several peptidase enzymes in Group N streptococci using gel filtration. Enzyme stability and the impact of nitrogen sources on enzyme elution were also investigated.

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    Area of Science:

    • Microbiology
    • Enzymology

    Background:

    • Group N streptococci are important bacteria with various enzymatic activities.
    • Peptidases play crucial roles in bacterial metabolism and protein turnover.

    Purpose of the Study:

    • To separate and identify peptidase activities in three species of Group N streptococci.
    • To investigate the stability of these enzymes under different conditions.
    • To examine the influence of growth medium composition on enzyme characteristics.

    Main Methods:

    • Gel filtration chromatography using Sephadex G-200 was employed for enzyme separation.
    • Characterization of enzyme stability involved varying temperature and pH.
    • Analysis of enzyme elution patterns was performed based on different nitrogen sources in the growth medium.

    Main Results:

    • Five distinct peptidase activities were identified: a general aminopeptidase, tripeptidase, proline iminopeptidase (prolyl-beta-napthylamidase), proline iminodipeptidase, and aminopeptidase-P.
    • Enzyme stability varied with temperature and pH.
    • The nitrogen source in the growth medium affected the elution patterns of the identified peptidases.

    Conclusions:

    • Group N streptococci possess a diverse range of peptidase activities.
    • Environmental factors like temperature, pH, and nutrient availability influence peptidase expression and stability.
    • Understanding these peptidases can provide insights into streptococcal physiology and metabolism.

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