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In an attempt to positively regulate meat quality at low NaCl concentration, the influence of L-histidine (L-his) introduction on the postmortem phosphorylation of chicken breast muscle protein that had been cured for 16 h at 1% NaCl was investigated at 90 min postmortem in the present study. The 633 different phosphoproteins (﹥1.2-fold) induced by L-his introduction during salting were identified, and a majority of these proteins were involved in glycolysis, calcium signalling pathway and muscle contraction. Myosin, actin, titin, troponin C (TnC), myosin light-chain kinase (MLCK) and γ-phosphorylase kinase (γ-PHK) were the main differentially expressed proteins (DEPs) that were associated with muscle contraction. An advantageous regulation of phosphoglucomutase-1 phosphorylation, fructose-1,6-bisphosphatase and pyruvate dehydrogenase E1 component was obtained in glycolytic metabolism after treatment with L-his.

The effect of a salt substitute (SS) containing L-lysine (Lys) and L-histidine (His) on secondary structure and gel properties of myosin from grass carp was examined. The results indicated that the α-helix content of myosin treated with SS was 29.00%, 29.03% and 35.93% more than that with NaCl at 0.4, 0.6 and 0.8 mol/L (P

This study evaluated the effect of substituting of NaCl with varying amounts of a combination of KCl, L-histidine (L-his), and L-lysine (L-lys) on the instrumental characteristics of cooked loin. Fifteen cooked loins were produced by replacing 0%, 25%, 50%, 75% and 100% of NaCl with the salt substitute. Experiments were conducted in triplicate to determine the water-holding capacity (WHC), and T2 relaxation time, and a texture profile analysis (TPA) and color determination test were also performed. T2 relaxation time analysis indicated that substitution affected the distribution of water by increasing the proportion of immobilized water and improving the WHC. results of TPA and color tests showed no adverse effect from using the experimental treatments. Results showed that 50% was the most suitable substitution ratio (actual 30.15% subsitution level of NaCl), for which the Na content was approximately 27% lower than that of the control for cooked loin.

The present study was designed to analyze the formation mechanics of heat-induced myofibrillar gels from rabbit psoas major at 0.6 mol/L KCl (pH 6.5) and 0.2 mol/L KCl (pH 6.0; n = 3). Morphological structure changes were observed using phase-contrast microscopy, transmission electron microscopy, scanning electron microscopy (SEM) and gel properties were determined through water-holding capacity (WHC), gel strength and dynamic rheological test. The results revealed that myofibrillar filaments aggregated and formed larger oligomers by side-by-side interactions when heated from 25 to 65°C. In higher ionic strength at higher pH, the filaments formed a more compact homogeneous network structure and the G′ value was much lower with higher WHC and gel strength, suggesting that the myofibril gel properties could be described by ∆G′. Based on the present study, it is suggested that the desired structural and textural attributes of myofibril gel can be manipulated by temperature, ionic strength and pH.