Manipulating interfacial behaviour and emulsifying properties of myofibrillar proteins by L‐Arginine at low and high salt concentration

Abstract

SummaryThe present work examined the impact of L‐Arginine (Arg) on the emulsifying properties, interfacial behaviour and conformational characteristics of myofibrillar proteins (MPs) at high (0.6 m) and low (0.15 m) salt concentration to maintain good emulsifying properties of MPs at low salt concentration. The data indicated that Arg increased the emulsifying activity index/emulsion stability index (EAI/ESI) and decreased the CI and droplet size of emulsions regardless of salt concentration. Raman spectra revealed that the α‐helix content decreased from 60.30% to 51.26% at high salt concentration, and from 60.20% to 54.82% at low salt concentration in the presence of Arg. In addition, MPs treated with Arg exhibited a higher interfacial pressure and more rapidly diffusion to the oil surface. Meanwhile, Arg increased the interfacial protein loading. The results demonstrated that Arg caused the unfolding of MPs, promoting the adsorption of proteins and decreasing the interfacial tension, ultimately improving the stability of emulsions at low salt concentration.