Characterization of the oligopeptides of Parmigiano-Reggiano cheese soluble in 120 g trichloroacetic acid/l

J Dairy Res. 1994 Aug;61(3):365-74. doi: 10.1017/s0022029900030788.

Abstract

The non-protein nitrogen (NPN) of samples of Parmigiano-Reggiano cheese ripened for 6 and 15 months was fractionated by ion-exchange chromatography on a Cu(2+)-Chelex column to separate oligopeptides from free amino acids. Peptide components were isolated by reversed-phase HPLC and identified by fast atom bombardment-mass spectrometry (FAB-MS). Only the NPN fraction of 6 month old cheese samples contained enough peptides to be further characterized. On the basis of FAB-MNS spectral results, 39 oligopeptides were identified, the main components being phosphopeptides. Two sets of both intact and partly dephosphorylated peptides, accounting for a total of 19 phosphopeptides, were formed by the hydrolysis of beta-casein and belonged to regions 1-20 and 6-28 of beta-casein. The formation and potential role of these peptides in cheese is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cheese / analysis*
  • Chromatography, High Pressure Liquid
  • Molecular Sequence Data
  • Molecular Weight
  • Oligopeptides / analysis*
  • Oligopeptides / chemistry
  • Phosphopeptides / analysis
  • Phosphopeptides / chemistry
  • Spectrometry, Mass, Fast Atom Bombardment

Substances

  • Oligopeptides
  • Phosphopeptides