The effect of three ingredients (triphosphate, lecithin and sucrose ester) on functionality and extractability of hake muscle proteins that had been intensely aggregated by frozen storage was investigated. Muscle proteins were extracted in 0.6M NaCl, 2% sodium dodecyl sulfate (SDS) and 2% SDS+5% (β‐mercaptoethanol (ME). Treatment with the added ingredients increased the amount of protein extracted when secondary interactions were broken with SDS. The same effect, although less pronounced, was found in the lots treated with triphosphate and sucrose ester when electrostatic bonds were broken with NaCl. The amphipathic ingredients (lecithin and sucrose ester) increased the amount of protein linked by nondisulfide covalent bonds.
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Huidobro et al. (1998) studied this question.
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