Nakamura Toshihide, Yoshida Ayako, Komatsuzaki Noriko, Kawasumi Toshiyuki, Shima Jun
National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan.
J Agric Food Chem. 2007 Jun 13;55(12):4871-6. doi: 10.1021/jf070069r. Epub 2007 May 22.
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.
为了研究一种酸面团特有的肽，从酸面团中提取了低分子量肽。将肽组分进行两种色谱法以分离肽。酸面团中肽组分的反相色谱显示出某些特定的肽。特定的肽组分通过凝胶过滤色谱进一步分离。液相色谱串联质谱分析鉴定其中一种肽为VPFGVG（六聚体）。该序列估计出现在低分子量谷蛋白亚基的287 - 292位。该肽（命名为SDP1）由小麦粉衍生的蛋白酶产生。SDP1显示出血管紧张素转换酶（ACE）抑制活性，50%抑制肽浓度（IC50）为336微摩尔。SDP1肽有可能在酸面团中部分赋予ACE抑制活性。
