Yuming Feng

Functional fish protein isolates prepared using low ionic strength, acid solubilization /precipitation

Abstract A technique was developed, whereby proteins from animal muscle tissue were solubilized under conditions of low ionic strength and low pH, that retained high yields of proteins, which when precipitated and neutralized were capable of producing gels with good functional properties. Gels made from acid-solubilized proteins commenced gelation at a substantially lower temperature when compared to washed muscle. Fluorescence data suggests extensive protein unfolding at pH values between 5.0 and 3.0, whereupon further acid addition in the range 3.0-2.0 resulted in a re-folding of the proteins. Extensive unfolding of the protein appears to be crucial to the development of a gel upon precipitation and neutralization.