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

- l-Arginine increased storage modulus, decreased phase angle.
- l-Arginine vanished the 1st and 3rd peak, but enhanced the enthalpy of the 2nd peak.
- l-Arginine favored to form a uniform gel and increased its water holding capacity.
- l-Arginine increased the proportion of relaxation populations centered at 43-351 ms.
- l-Arginine showed the potential in the manufacture of meat products.

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 0-0.25 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 (G′), but decreased phase angle (tan δ). 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 (ΔH2). Low field nuclear magnetic resonance (LF-NMR) showed l-Arg at 0.25 g/100 g increased the fraction of spin-spin 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.