ABSTRACTEnzymemodified acylated protein derivatives were prepared with succinic and acetic anhydrides from washed fish muscle and were evaluted for their functionality. The degree of acylation and of hydrolysis by bromelain was studied to determine how these variables affect functionality of the protein. The degree of acylation was determined by measuring available epsilon amino groups of lysine. Susceptibility to hydrolysis was determined by treating with bromelain at different ratios of bromelain to substrate. The functional properties studied were emulsifying activity, emulsifying capacity, gelation, water absorption, aeration, and foam stability. These functional properties increased until 43–59 of the free amino groups were acylated. Further acylation had no significant effect. Hydrolysis of the acylated protein slightly lowered the emulsifying, gelation, and water absorption properties, but increased the aeration capacity of both the acetylated and succinylated proteins and the foam stability of the latter. The succinylated proteins displayed functional properties similar to those of the acetylated proteins. Succinylated proteins, however, yielded functionality slightly but significantly superior to that of acetylated proteins. The performance of enzyme‐modified acylated fish protein derivatives in food systems is also discus
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