Protein concentrates and isolates have been produced on a large scale to serve as functional ingredients in a wide and ever increasing range of application in foods. The objective of this work was to evaluate the solubility, water holding capacity (WHC) and oil holding capacity (OHC). The process of acid and alkaline solubilization the triturated fillets (approximately 200 g) was homogenized in proportion of 1:9 (w/v) with distilled water at 4° C for 60 sec. The protein solubilization was performed at 4°C in temperature controlled by an ultrathermostatic bath for 20 minutes under constant stirring with a propeller shaft stirrer. Solubilization of protein was performed with 1N HCl and 1N NaOH at pH 2,8 and 11 respectively, for 20 min, then centrifuged at 9000 x g for 20 min. Soluble proteins were subjected to isoelectric precipitation (pH 5.0) with addition of 1 N HCl solution or 1 N NaOH; a second centrifugation was performed at 9000 xg for 20 min, where the precipitate called protein isolate. The solubility values, at pH 5 both had high values, with basic protein isolates (BPI) being higher, and at pH 7 the lowest values, with BPI lower than acidic protein isolates (API).The WHC 26 mL water/g protein was obtained for API, and 15 mL water/g protein for BPI are between pH 5 and pH 7, since these are closer to the isoelectric point of the protein. At pHs below 5.0 and above 7.0, water molecules combine with the polar groups of proteins and the WHC tends to increase. The mean OHC obtained for BPI was 6.30 ± 0.48 (mL of oil/g protein) while for API this was 6.14 ± 0.05 (mL of oil/g protein). Both isolates had good functional properties, however, the basic protein isolate showed better results.