Phospholipase and proteinase activities in different Candida species isolated from anatomically distinct sites of healthy adults.
The aim of the present study was to determine in vitro phospholipase and protease activities in 122 Candida spp. isolated from several anatomically distinct sites of healthy adults. C. albicans (66.4%) was the most frequently isolated Candida spp. C. glabrata (7.3%), C. tropicalis (6.3%) and C. kefyr (4.9%) were the most frequently isolated non-C. albicans Candida spp. Fifty (40.9%) of the isolates examined were phospholipase positive and 64 (52.4%) were protease positive. Forty-three (53.8%) of the C. albicans isolates tested were phospholipase producers--however, only a few strains of non-C. albicans Candida spp. behaved in the same way. Protease activity was detected in 46 (56.7%) of the C. albicans strains tested and in a few strains of non-C. albicans Candida spp. The levels of phospholipase and protease activities in commensal isolates were found to be lower than the levels of other enzyme activities previously reported in clinical Candida spp. isolates. The phospholipase activity of Candida spp. was found to be higher in oral (59.0%) and fecal (42.8%) isolates. The protease activity of Candida spp. was found to be higher in urogenital (55.1%) and skin (58.8%) isolates. We conclude that further investigations will be needed on the phospholipase and protease activity of Candida spp. in healthy subjects in order to clarify their contribution to fungal virulence.
Oksuz
Sukru
S
Department of Microbiology and Clinical Microbiolgy, Duzce Ataturk State Hospital, Duzce, Turkey. droksuz@gmail.com
Sahin
Idris
I
Yildirim
Mustafa
M
Gulcan
Aynur
A
Yavuz
Tevfik
T
Kaya
Demet
D
Koc
Ayse Nedret
AN
D000328:Adult; D002175:Candida / Q000201:enzymology* / Q000302:isolation & purification; D005243:Feces / Q000382:microbiology; D005260:Female; D006801:Humans; D008297:Male; D009055:Mouth / Q000382:microbiology; D010447:Peptide Hydrolases / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism*; D012867:Skin / Q000382:microbiology; D014566:Urogenital System / Q000382:microbiology
D010740:Phospholipases; D010447:Peptide Hydrolases