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Effects of L-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

Effects of L-Arginine on water holding capacity and texture of
heat-induced gel of salt-soluble proteins from breast muscle


Abstract


The paper focused on the effects of L-Arginine (L-Arg) on the water holding capacity (WHC) and texture of salt-soluble meat proteins (SSMP) gel and the thermal gelling mechanism were investigated. The addition of 0e0.25 g L-Arg/100 g increased the WHC, hardness, springiness cohesiveness and chewiness of SSMP gel. Rheology indicated the addition of L-Arg increased storage modulus (G0), but decreased phase angle (tan d). Differential scanning calorimeter (DSC) disclosed that L-Arg-treatment caused the disappearance of the first and third transition peaks, but the increase of the enthalpy of the second denaturation (DH2). Low field nuclear magnetic resonance (LF-NMR) showed L-Arg at 0.25 g/100 g increased the fraction of spinespin relaxation times distribution for immobile water (T21). Scanning electron microscopy (SEM) revealed that L-Arg promoted to form a dense, uniform SSMP gel. The results suggested that the thermal stability and gelation of SSMP were affected by L-Arg, which changed the microstructure of SSMP gel, and ultimately improving the corresponding WHC and texture, as well as changing the distribution of T2.

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