The physicochemical and gelation properties of salt‐soluble proteins (SSP) extracted from chicken muscles were studied at 0.6M NaCl, pH 6.00. Thermally induced protein unfolding and protein‐protein interaction were determined by 8‐anilino‐1‐naphthalene sulfonate (ANS) fluorescence and turbidity. Breast and leg SSP showed similar changes in protein unfolding, but differed in protein‐protein interactions. Post‐rigor breast SSP formed stronger and more elastic gels than prerigor breast and pre and postrigor leg SSP. Leg SSP gelation was less affected by muscle rigor state than breast SSP. Protein conformational changes were concluded to precede SSP association, which was a prerequisite for gel formation.
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Xiong et al. (1990) studied this question.
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