Protein solubility of whole and minced muscle of hake (Merluccius merluccius L.) was evaluated at different temperatures of storage:-5°,-12° and-20°C. Proteins soluble in 1% NaCl did not show any change at any of the temperatures of storage, while the 5% NaCl-soluble proteins decreased significantly when whole hake was stored at-5° and-12°C (p < 0.01). A correlation was found between the decrease of solubility and the production of formaldehyde at-5° and-12°C (p < 0.001 and p < 0.01, respectively). Bound formaldehyde (formaldehyde not extractable) increased with storage time at-5° (p < 0-001). The addition of formaldehyde to the minced muscle brought about a decrease in both the 1% and the 5% NaCl-soluble proteins. The decrease was dependent upon the temperature, the amount of formaldehyde added and the time of storage. The role of formaldehyde in the denaturation of sarcoplasmic proteins was confirmed by measuring trimethylamino oxide demethylase activity during the experiment.