[Persistent properties of microorganisms inhabiting highly mineralized water bodies]

Zh Mikrobiol Epidemiol Immunobiol. 2012 Jul-Aug:(4):62-6.
[Article in Russian]

Abstract

Aim: Study prevalence and intensity of persistent properties in bacteria inhabiting highly min eralized water bodies and determine their role in interaction with halophilous heterotrophic protozoa.

Materials and methods: 300 bacteria strains and 3 cultures of heterotrophic protozo isolated from water bodies with mineralization of 2-350 g/l were studied. Antilysozyme (ALA) antihistone (AHA) activity of bacteria, protozoa lysozyme were evaluated by dish and photometric methods. Protozoa histones were evaluated cytochemically. Interaction of protozoa and Escherichia coli was evaluated by experimental co-cultivation.

Results: Presence of lysozyme an histones was shown in halophilous heterotrophic protozoa. Prevalence of ALA and AHA in bacteria was shown to increase as water body mineralization decreases. Intensity of E. colielimination from brine was determined to depend on the bacteria ALA level and phagocytic activity of protozoa. Participation of halotolerant protozoa in formation of heterogeneity of bacterial population by ALA was shown.

Conclusion: In biocenoses of highly mineralized water bodies functioning of lysozyme-antilysozyme, histone-antihistone systems was shown. Bacteria with high persistent potential may impair sanitary parameters of highly mineralized water bodies, process of self-purification of which depends directly on phagocytic activity of protozoa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biota
  • Escherichia coli / physiology*
  • Euglenida / physiology*
  • Fresh Water / microbiology*
  • Heterotrophic Processes
  • Histones / analysis
  • Histones / antagonists & inhibitors
  • Minerals / chemistry
  • Muramidase / analysis
  • Muramidase / antagonists & inhibitors
  • Phagocytes / physiology
  • Phagocytosis / physiology
  • Water Microbiology*

Substances

  • Histones
  • Minerals
  • Muramidase