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Fish protein was acylated with acetic anhydride(AA), succinic anhydride(SA) and malefic anhydride(MA) in order to improve the functional properties of the protein. The surface hydrophobicity and functional properties of protein were measured to study the relationship between them. It was found that the extented acylation of nucleophilic groups such as amino and sulfhydryl groups of the amino acid residues of fish protein was higher than other groups when acylated with AA, and the degree of acylation was 89.5 3b for amino groups and 72.2 % for sulfhydryl groups. The surface hydrophobicity of fish protein was decreased by succinylation and maleylation, whereas acetylation caused Little change. The acylated fish protein concentrate(FPC) showed higher surface hydrophobicity than the acylated fish myofibrilla protein(FMP). Acylation with AA, SA and MA of fish protein resulted in a significant increase in protein solubility, emulsifier properties, foaming properties, water adsorption capacity and oil adsorption capacity. These properties of acylated FMP were more improved than those of acylated FPC. Decrease in protein hydrophobicity was highly correlated with increase in protein solubility, and emulsifier properties and foaming properties were largely dependent on the solubility as well as surface hydrophobicity. The water adsorption capacity of the protein was significantly affected by solubility. Surface hydrophobicity had greater influence on oil adsorption capacity, whereas it had little effect on water adsorption capacity.
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