ABSTRACT: Channel catfish muscle was subjected to 2 novel protein extraction and precipitation techniques using acid (pH 2.5) or alkaline (pH 11) pH and compared with surimi processing (3 wash cycles). Solubility of catfish proteins was found to be highest at pH 2.5 and 11, and at these pH levels, viscosity was found to be low enough to cause separation of proteins from insoluble materials via centrifugation. Both the acid-aided and alkali-aided processes led to higher recoveries (P < 0.05) of protein and larger reduction (P < 0.05) in lipids compared with surimi processing. The protein recovery could be increased even more with a modified version of the acid-aided and alkali-aided processes. There was no hydrolytic breakdown detected during low and high pH. The acid-aided process recovered more protein types than the alkali-aided process during isolelectric precipitation (pH 5.5), which indicated that it led to more protein denaturation and thus more aggregation at pH 5.5. The alkali-aided process had more soluble proteins (including heme proteins) at isoelectric precipitation than the acid-aided process, and the soluble proteins were of the same type as the soluble proteins for non-pH-treated catfish muscle at pH 5.5. This suggested the alkali-aided process led to less denaturation than the acid-aided process. Both acid-aided and alkali-aided processes recovered proteins of higher (P < 0.05) whiteness scores than surimi. The alkali-aided process recovered proteins of higher whiteness (P < 0.05) than the acid-aided process. The acid-aided process led to higher yellowness (P < 0.05) than the other 2 processes. All processes led to minimal levels of lipid oxidation as assessed by secondary oxidation products.