Metal solubility enhancing peptides derived from barley protein

Food Chem. 2014 Sep 15:159:498-506. doi: 10.1016/j.foodchem.2014.03.061. Epub 2014 Mar 20.

Abstract

Mineral supplements are required to be soluble as their bioavailability is highly correlated to their solubility in body fluids. In this study, metal binding capacity of barley protein hydrolysates and their purified fractions was investigated and expressed as increase in solubility of metal ions. Metal ions in the presence of hydrolysates exhibited a remarkable increase in solubility: 118, 32, 10, 29 and 35-fold for Fe(2+), Fe(3+), Ca(2+), Cu(2+) and Zn(2+), respectively. A mixture of low molecular weight peptides possesses a synergistic combination of both charged and hydrophobic residues and achieves the best binding metal ions. Electrostatic interactions via charged side chains and coordination binding with His and Cys, initially attract the metal ions and, afterward, hydrophobic interactions and aromatic ring stacking stabilize the positioning of metal ions in the structure of the peptide. Barley hordein hydrolysates show potential as dietary supplements that enhance both mineral solubility and bioavailability.

Keywords: Barley protein hydrolysate; Enhanced metal solubility; Metal binding; Peptide structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry
  • Chromatography, High Pressure Liquid
  • Food Analysis / methods*
  • Glutens / chemistry*
  • Hordeum / chemistry*
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Hydrophobic and Hydrophilic Interactions
  • Ions / chemistry
  • Metals / chemistry*
  • Molecular Weight
  • Peptides / chemistry
  • Protein Hydrolysates / chemistry*
  • Salts / chemistry
  • Solubility
  • Static Electricity
  • Ultrafiltration

Substances

  • Amino Acids
  • Ions
  • Metals
  • Peptides
  • Protein Hydrolysates
  • Salts
  • Glutens