PL
Celem pracy była ocena biochemicznych i enzymatycznych właściwości szczepów C. amycolatum. W grupie 70 badanych szczepów wyróżniono 21 profili biochemicznych, wśród których dominował biotyp 310032S (35,7%). Prawie wszystkie szczepy fermentowały glukozę (98,6%) i maltozę (95,7%) oraz wytwarzały pyrazynamidazę (94,3%). Wszystkie wytwarzały fosfatazę alkaliczną i fosfohydrolazę, a 95,7% — fosfatazę kwaśną. Żaden szczep nie wykazywał właściwości proteolitycznych, aktywności lipazy/lecytynazy i nie hydrolizował Tweenu 80.
EN
C. amycolatum is the most commonly isolated nonlipophilic species of Corynebacterium from clinical samples. However, the lack of good commercial identification tests in microbiology laboratories causes some difficulties in C. amycolatum diagnostics. We decided to examine biochemical and enzymatic properties of isolated strains and analize occurrence of particular biochemical profiles (biotypes). Perhaps it would let improve the identification schemes. 70 strains of C. amycolatum were analized. The estimation of biochemical properties consisted of the results of API Coryne and API ZYM tests (bioMérieux), the ability of excreting of protease, esterase, lipase and lecithinase. Analized strains had various biochemical and enzymatic properties. Almost all strains fermented glucose (98,6%) and maltose (95,7%) and producted pyrasinamidase (94,3%). All strains producted alkaline phosphatase and phosphohydrolase, and 95,7% — acid phosphatase. Biotypes of particular strains were determined on the biochemical reactions included in the API Coryne tests. In the group of 70 strains 21 profiles were distinguished among which 3100325 biotype (35,7%) was dominant. The lipolysis was defined on Tween 20, Tween 40, Tween 60, Tween 80 medium and with the API ZYM test usage. All strains producted esterase-lipase (esterase C-8), 95,7% of strains-esterase C-4, and 21,4% lipase C-14. Among analized strains 18,6% hydrolyzed Tween 20, 14,3% Tween 60, and 1,4% Tween 40. None of these strains demonstrated lipase and lecithinase activity. Difficulties in concerning C. amycolatum as pathogens justify further investigations.