Candida parapsilosis is an emerging fungal pathogen implicated in many diseases, especially in compromised hosts. In most parts of the world is the third most common cause of  candidemia. In the present study, a surface ecto-phosphatase was identified in C. parapsilosis yeast cells. Intact yeasts hydrolyzed p-NPP at a rate of 24.30 ± 2.6 nmol   p-NP / h x 10⁷ cells. A finding compatible with an acid phosphatase was detected when activity was decreased at alkaline pH range and inhibited in a dose-dependent manner by classical inhibitors of this kind of enzymes. However, only the inhibition of enzyme activity caused by sodium orthovanadate has been shown to be irreversible. This activity was also reversible inhibited by exogenous inorganic phosphate (Pi). Accordingly, removal of Pi from the culture medium resulted in a marked increase of the phosphatase activity. The ecto-phosphatase present in C. parapsilosis hydrolyzed several substrates such as p-NPP, b-glycerophosphate, α-naftylphosphate, phosphotyrosine, phosphothreonine and phosphoserine with different rates. Similar to that observed for phosphotyrosine phosphatases, the phosphatase activity in C. parapasilosis was stimulated by Cu²⁺ and inhibited by Zn²⁺. In addition, reductive agents as DTT, β-mercaptoethanol and suicide amino acids as cystein, histidine and serine were tested and the results indicate that Cu²⁺ and Zn²⁺ affects the sulphydrile residues in ecto-phosphatase. Surface  phosphatase activity was apparently involved on the early mechanisms required for disease establishment and we also observed that strains recently isolated  showed increased enzymatic activity when compared with a laboratory-adapted strain. Taken together, these observation suggest a link between ectophosphatase activity and fungal parasitism.