Abstrakt

Most of the Earth’s biosphere is permanently or periodically exposed to temperatures below 5°C. Cold habitats harbor a wide diversity of psychrophiles. For many years Antarctica has been the geographic area preferred for studying the diversity and properties of cold-adapted microorganisms. However, the non-Antarctic habitats like Himalayas or Alps are also extensively explored. The Tatra Mountains are Europe’s second-highest massif after the Alps. The Polish part of the Tatras has tens caves. The microclimatic conditions in the Tatra caves are very severe, with temperature ranging from below freezing to a maximum of 6°C. AIM. The aim of this study was isolation and characterization of yeasts that inhabit selected caves of the Polish Tatras. MATERIALS AND METHODS. Samples of water were collected in the Zimna Cave, Wielka Śnieżna Cave, Miętusia Cave and Kasprowa Niżnia Cave. Yeasts were isolated by growing on agar plates supplemented with ampicillin and chloramphenicol. The effect of temperature was examined at 5-37°C. Assimilation of carbon and nitrogen compounds were tested at 18°C. The proteolytic activity was examined on agar plates containing milk. Other enzymatic activities were tested using API ZYM. Isolates were identified by analysis of D1/D2 sequences of 26S rDNA. RESULTS. Nine yeast strains were isolated from water samples collected in four Tatra caves. Six of them were considered as psychrotolerants. Only one cold-adapted isolate belongs to the ascomycetous yeasts and it was classified as Candida sake. The psychrotolerant basidiomycetous yeasts were identified as Guehomyces pullulans, Rhodotorula glutinis or Cystofilobasidium capitatum. Two yeast strains had biotechnological potential. R. glutinis exhibited high proteolytic activity, whereas G. pullulans was able to produce β-galactosidase and α-amylase. CONCLUSIONS. The Tatra Mountains are the geographic region useful for studying the diversity and properties of cold-adapted microorganisms. The isolated strains can have biotechnological potential, e.g. as sources of cold-active enzymes.

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