Isolation and characterization of a low molecular weight peptide contained in sourdough.

To investigate a sourdough-specific peptide, low molecular weight peptides were extracted from sourdough. The peptide fraction was subjected to two kinds of chromatography to separate the peptides. Reverse-phase chromatography of the peptide fraction in the sourdough showed certain specific peptides. The specific peptide fraction was further separated by gel filtration chromatography. Liquid chromatography tandem mass spectrometry analysis identified one of the peptides as VPFGVG (six-mer). This sequence was estimated to occur at the 287-292 position of a low molecular weight glutenin subunit. The peptide (designed as SDP1) was produced by proteases derived from wheat flour. SDP1 showed angiotensin-converting enzyme (ACE) inhibitory activity, and the 50% inhibitory peptide concentration (IC50) was 336 microM. It is possible that the SDP1 peptide partially confers ACE inhibitory activity in sourdough.