l–Arginine and l–Lysine improve the physical stability of soybean oil–myosin emulsions by changing penetration and unfolding behaviors of interfacial myosin

Multifaceted functionality of l-arginine in modulating the emulsifying properties of pea protein isolate and the oxidation stability of its emulsions

“…Correspondingly, the contents of β-sheet and random coil structures reached their highest content-15.91% and 34.29%, respectively. These findings were similar to the previously reported changes in the secondary structure of whey protein 22 and myofibrillar protein 23 induced by Arg, indicating that treatments with suitable concentrations of Arg can induce protein structure expansion and flexibility enhancement. 14 However, when the Arg concentration was in the range of 0.2%-1.0% the proportion of α-helix structure increased while that of β-sheet structure decreased.…”

“…This journal is © The Royal Society of Chemistry 2022 amphiphilic molecule to stabilize the interface protein. 23 It is worth noting that, with an increase in arginine concentration from 0.2% to 1.0%, the EAI of PPI showed a significant downward trend although the EAI of PPI with 0.5% or 1.0% Arg was still higher than that of the control. One possible reason is that excessive Arg might have led to negative competitive adsorption with the protein at the oil-water interface, reducing the EAI of PPI.…”

“…The maximum EAI of A-PPI was found to be 10.91 m 2 g −1 at 0.2% Arg, which was 28.35% higher than that of the control (P < 0.05). Similarly, Li et al 23 showed that the addition of Arg could significantly improve the EAI of salt-soluble meat proteins. The increase of EAI in A-PPI can be attributed to two reasons: (1) The presence of Arg could have enhanced the charge repulsion, inhibiting PPI aggregation and improving protein solubility (Fig.…”

“…One possible reason is that excessive Arg might have led to negative competitive adsorption with the protein at the oil-water interface, reducing the EAI of PPI. 23 Therefore, treatment with an appropriate concentration (0.2%) of Arg was conducive to improving the emulsifying ability of PPI.…”

“…It was also reported that Arg could assist β-lactoglobulin crosslinking to form a homogeneous and porous three-dimensional network structure, leading to an improvement in the water-holding capacity of the protein gels. 22 Li et al 23 demonstrated that the addition of 0.2% Arg induced the structural expansion of myosin, promoted the rearrangement and localization of myosin on the surface of oil droplets, and promoted the interaction with the oil droplets, thereby improving the emulsifying activity of myosin and the stability of the myosin-soybean oil emulsion system. However, there is no published literature on how Arg regulates the structural and functional properties of PPI.…”