Based on hydrogen and disulfide-mediated bonds, l-lysine and l-arginine enhanced the gel properties of low-salt mixed shrimp surimi (Antarctic krill and Pacific white shrimp)

Food Chem. 2024 Jul 1:445:138735. doi: 10.1016/j.foodchem.2024.138735. Epub 2024 Feb 12.

Abstract

This study delved into the effects of l-lysine (Lys) and l-arginine (Arg) on the gel properties and intermolecular interactions of low-salt (NaCl, 1 g/100 g) mixed shrimp surimi (Antarctic krill and Pacific white shrimp). The addition of Lys and Arg improved the gel strength and water holding capacity of low-salt gels, which were superior to the properties of STPP and high-salt (NaCl, 2.25 g/100 g) gels. These results can be attributed to the role of Lys and Arg in enhancing hydrogen and disulfide bonds within the low-salt gel system, promoting the solubilization of myofibrillar proteins (MP) and consequently increasing the number of MP molecules participating in gel formation. Antarctic krill MP did not show gel-forming ability and exerted a diluting effect on low-salt mixed shrimp surimi gels. Molecular docking analysis indicated the stable binding of Lys and Arg to myosin.

Keywords: Antarctic krill; Gel properties; Low-salt; Myofibrillar proteins; l-arginine; l-lysine.

MeSH terms

  • Animals
  • Arginine
  • Disulfides
  • Euphausiacea*
  • Fish Proteins / chemistry
  • Gels / chemistry
  • Lysine
  • Molecular Docking Simulation
  • Proteins
  • Sodium Chloride*
  • Sodium Chloride, Dietary

Substances

  • Sodium Chloride
  • Lysine
  • Gels
  • Proteins
  • Sodium Chloride, Dietary
  • Arginine
  • Disulfides
  • Fish Proteins