Use of l-arginine-assisted ultrasonic treatment to change the molecular and interfacial characteristics of fish myosin and enhance the physical stability of the emulsion

Food Chem. 2021 Apr 16:342:128314. doi: 10.1016/j.foodchem.2020.128314. Epub 2020 Oct 7.

Abstract

The effects of l-arginine (Arg)-assisted ultrasonic treatment on the molecular and interfacial characteristics of myosin and emulsifying properties of the emulsion were evaluated to ascertain the underlying mechanism in improving the emulsion stability. Ultrasonication induced the exposure of residues of native myosin, which was increased by the addition of Arg (40 mM). Furthermore, in terms of emulsions containing Arg, the higher the ultrasonication intensity was, the greater the increase in adsorbed protein (from 15.43 ± 0.28% to 50.49 ± 1.65%) and π value, and the decrease in droplet sizes (from 4098 nm to 2324 nm) (P < 0.05). Moreover, the increase in the ordered structures of interfacial myosin induced by Arg and ultrasonication favoured the formation of a protein gelation network. In summary, Arg-assisted ultrasonic treatment improved the stability of the emulsion by inducing the exposure of native myosin and facilitating the formation of ordered structures of interfacial myosin.

Keywords: Arg; Aromatic and aliphatic amino acid residues; Emulsion; Protein gelation network; Stability; Ultrasonication.

MeSH terms

  • Adsorption
  • Animals
  • Arginine / chemistry*
  • Emulsions / chemistry*
  • Fish Proteins / chemistry*
  • Gels
  • Myosins / chemistry*
  • Sonication*

Substances

  • Emulsions
  • Fish Proteins
  • Gels
  • Arginine
  • Myosins