title: Phospholipase and proteinase activities in different Candida species isolated from anatomically distinct sites of healthy adults.
abstract: 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.
authors: Department of Microbiology and Clinical Microbiolgy, Duzce Ataturk State Hospital, Duzce, Turkey. droksuz@gmail.com
authors: Sukru
authors: S
authors: Oksuz
authors: Idris
authors: I
authors: Sahin
authors: Mustafa
authors: M
authors: Yildirim
authors: Aynur
authors: A
authors: Gulcan
authors: Tevfik
authors: T
authors: Yavuz
authors: Demet
authors: D
authors: Kaya
authors: Ayse Nedret
authors: AN
authors: Koc
mesh_terms: 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
chemical_list: D010740:Phospholipases; D010447:Peptide Hydrolases