Functional and Rheological Properties of Vicia faba L. Protein Isolates

Biomolecules. 2021 Jan 28;11(2):178. doi: 10.3390/biom11020178.

Abstract

A protein isolate (85.5%) was obtained from the Vicia faba L. seeds. The main protein fraction, typical for the seeds of this plant, was found to be most numerous: Legumin (35 kDa) and Vicilin (45 kDa). The hydrodynamic and surface properties of isolate aqueous solutions were studied with the help of dynamic light scattering, ζ-potential, and tensometry in a wide range of concentrations and pH conditions. Selected functional properties, like foaming and emulsifying abilities, were studied. An increase of water solubility was shown with a raising pH, as well as a water holding capacity (WHC). The protein isolate showed a tendency to decrease the surface tension of water solutions, with high hydrophobicity and a negative charge of the isolate enhancing the foaming and emulsifying properties. The analysis of the concentration and the pH influence on selected functional properties indicated alkaline conditions as favorable for good foaming and emulsifying properties of the isolate and affected on their rheological properties.

Keywords: Vicia faba L. seeds; functional properties; protein isolates; rheology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Emulsions
  • Fabaceae
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Legumins
  • Light
  • Plant Proteins / chemistry*
  • Plant Proteins / metabolism
  • Rheology
  • Scattering, Radiation
  • Seed Storage Proteins / chemistry*
  • Seeds / chemistry
  • Solubility
  • Surface Properties
  • Surface Tension
  • Temperature
  • Vicia faba / metabolism*
  • Water

Substances

  • Emulsions
  • Plant Proteins
  • Seed Storage Proteins
  • Water
  • vicilin protein, plant