TY - JOUR
T1 - Physicochemical and Gelation Properties of Pre‐ and Postrigor Chicken Salt‐soluble Proteins
AU - XIONG, Y. L.
AU - BREKKE, C. J.
PY - 1990/11
Y1 - 1990/11
N2 - 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.
AB - 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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U2 - 10.1111/j.1365-2621.1990.tb03564.x
DO - 10.1111/j.1365-2621.1990.tb03564.x
M3 - Article
AN - SCOPUS:84985200141
SN - 0022-1147
VL - 55
SP - 1544
EP - 1548
JO - Journal of Food Science
JF - Journal of Food Science
IS - 6
ER -