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Trichomonas tenax proteolytic activity

S Segović1, D Buntak-Kobler, N Galić

  • 1Department of Dental Pathology, School of Dentistry, University of Zagreb.

Collegium Antropologicum
|February 10, 1999
PubMed
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Proteolytic enzymes from Trichomonas tenax in dental plaque were analyzed. These enzymes show activity at different pH levels, with peak effectiveness at 36 kDa, indicating diverse endopeptidases.

Area of Science:

  • Microbiology
  • Biochemistry
  • Parasitology

Background:

  • Trichomonas tenax is a protozoon found in oral cavities.
  • Its role in oral health, particularly in dentobacterial plaque, requires further investigation.
  • Understanding its enzymatic activity is crucial for assessing its pathogenic potential.

Purpose of the Study:

  • To investigate the proteolytic activity of Trichomonas tenax.
  • To characterize the optimal conditions for this enzymatic activity.
  • To identify potential endopeptidases present in Trichomonas tenax.

Main Methods:

  • Proteolytic activity was analyzed using electrophoretic methods.
  • Polyacrylamide gels stained with Coomassie Brilliant Blue R-250 were employed.

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  • Gelatin-containing polyacrylamide gels were used to detect protease activity.
  • Enzyme activity was assessed across different pH levels (2.8, 4.6, 5.6).

    • Main Results:

    • Significant proteolytic activity was observed in Trichomonas tenax from dentobacterial plaque.
    • Optimal activity occurred at pH 4.6, followed by pH 5.6.
    • Activity was also detected, though less effective, at pH 2.8.
    • The most prominent proteolytic activity was associated with a protein molecular weight of 36 kDa.

    Conclusions:

    • Trichomonas tenax possesses diverse proteolytic enzymes.
    • The pH-dependent activity suggests the presence of multiple endopeptidases.
    • These findings contribute to understanding the biochemical capabilities of Trichomonas tenax in the oral environment.