Abstract
A fish protein hydrolysate (FPH) from Pacific whiting (Merluccius productus) muscle was produced by autolysis of a minced homogenate (8% protein) at pH 7.0 and 60°C, where maximum endogenous proteolytic activity was detected. FPH production was controlled by the pH stat method, yielding a 4.43% degree of hydrolysis after 1 h of autolysis. Upon autolytic processing, 28.9 ± 0.7% of the total protein was found in the soluble fraction. FPH was 100% soluble at pH 7.0 and 10.0 and was less soluble at pH 4 (82.5%, P ≤ 0.05). FPH showed better emulsifying properties than sodium caseinate (SCA) at pH 4.0 (P ≤ 0.05), but had a lower foaming capacity (P ≤ 0.05) than bovine albumin (BSA) at all evaluated pHs. FPH foaming capacity was not affected by pH, however, foam stability was equal or better than that of BSA, especially at pH 4.0 (P ≤ 0.05). These results suggest the possibility of producing FPH with similar or better functional properties than those of functional ingredients, such as SCA and BSA. Furthermore, the data presented support our hypothesis that the high proteolytic activity in Pacific whiting could be used as an advantage in fish protein hydrolysate production or as a processing aid where protein hydrolysis is required.
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