TY - JOUR
T1 - Morphological examinations of oxidatively stressed pork muscle and myofibrils upon salt marination and cooking to elucidate the water-binding potential
AU - Liu, Zelong
AU - Xiong, Youling L.
AU - Chen, Jie
PY - 2011/12/28
Y1 - 2011/12/28
N2 - Pork longissimus muscle samples were subjected to the following three marination conditions: (A) oxidation (40 min) in hydroxyl radical-generating solutions (HRGS; 10 μM FeCl 3/100 μM ascorbate with 5 or 20 mM H 2O 2, pH 6.2) containing 0.1 M NaCl and then marination (40 min) in 0.6 M NaCl with 15 mM pyrophosphate (PP); (B) simultaneous oxidation/marination (40 min) in HRGS containing 0.6 M NaCl and 15 mM PP; or (C) the same as condition B except that PP was omitted. Protein oxidation, measured by the carbonyl and tryptophan fluorescence changes, enhanced hydration but increased cooking loss of meat. Light microscopy revealed a dense muscle structure characterized by swollen fibers and reduced intercellular spacing in intermediately oxidized muscle samples marinated with 0.6 M NaCl and 15 mM PP. However, oxidized fibers were more susceptible to transverse shrinkage upon cooking than nonoxidized fibers, which was supported by the dynamic ultrastructural changes in myofibrils observed using phase contrast microscopy. These findings provide a further understanding of the complex impact of oxidation on meat hydration and water-binding.
AB - Pork longissimus muscle samples were subjected to the following three marination conditions: (A) oxidation (40 min) in hydroxyl radical-generating solutions (HRGS; 10 μM FeCl 3/100 μM ascorbate with 5 or 20 mM H 2O 2, pH 6.2) containing 0.1 M NaCl and then marination (40 min) in 0.6 M NaCl with 15 mM pyrophosphate (PP); (B) simultaneous oxidation/marination (40 min) in HRGS containing 0.6 M NaCl and 15 mM PP; or (C) the same as condition B except that PP was omitted. Protein oxidation, measured by the carbonyl and tryptophan fluorescence changes, enhanced hydration but increased cooking loss of meat. Light microscopy revealed a dense muscle structure characterized by swollen fibers and reduced intercellular spacing in intermediately oxidized muscle samples marinated with 0.6 M NaCl and 15 mM PP. However, oxidized fibers were more susceptible to transverse shrinkage upon cooking than nonoxidized fibers, which was supported by the dynamic ultrastructural changes in myofibrils observed using phase contrast microscopy. These findings provide a further understanding of the complex impact of oxidation on meat hydration and water-binding.
KW - Muscle oxidation
KW - cooking
KW - hydration properties
KW - marination
KW - morphology
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U2 - 10.1021/jf2041017
DO - 10.1021/jf2041017
M3 - Article
C2 - 22084832
AN - SCOPUS:84255186211
SN - 0021-8561
VL - 59
SP - 13026
EP - 13034
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 24
ER -