Iron-binding properties of sugar cane yeast peptides

Food Chem. 2014 Jan 1:142:166-9. doi: 10.1016/j.foodchem.2013.06.133. Epub 2013 Jul 18.

Abstract

The extract of sugar-cane yeast (Saccharomyces cerevisiae) was enzymatically hydrolysed by Alcalase, Protex or Viscozyme. Hydrolysates were fractionated using a membrane ultrafiltration system and peptides smaller than 5kDa were evaluated for iron chelating ability through measurements of iron solubility, binding capacity and dialyzability. Iron-chelating peptides were isolated using immobilized metal affinity chromatography (IMAC). They showed higher content of His, Lys, and Arg than the original hydrolysates. In spite of poor iron solubility, hydrolysates of Viscozyme provided higher iron dialyzability than those of other enzymes. This means that more chelates of iron or complexes were formed and these kept the iron stable during simulated gastro-intestinal digestion in vitro, improving its dialyzability.

Keywords: Dialyzability; Immobilized metal affinity chromatography; Iron-chelating peptides; Protein hydrolysates; Sugar-cane yeast.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Iron / chemistry
  • Iron-Binding Proteins / chemistry*
  • Iron-Binding Proteins / isolation & purification
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Protein Binding
  • Protein Hydrolysates / chemistry
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / isolation & purification
  • Subtilisins / chemistry

Substances

  • Iron-Binding Proteins
  • Peptides
  • Protein Hydrolysates
  • Saccharomyces cerevisiae Proteins
  • Iron
  • Subtilisins