本みりんのアンジオテンシンI変換酵素(ACE)阻害活性を有するペプチドについて

概要

論文の詳細を見る
We had previously found that mirin exhibited angiotensin I converting enzyme (ACE) inhibitory activity, and therefore investigated the ACE inhibitors from mirin. In the first step, a mirin solution was subjected to ion-exchange chromatography and separated into its basic nitrogen, acidic-neutral nitrogen, acidic, and neutral substance fractions. Almost all the overall ACE inhibitory activity was found in the acidic-neutral nitrogen fraction. In the second step, this acidic-neutral nitrogen fraction was fractionated by gel filtration, and each fraction was individually collected. In the third step, the collected fraction from gel filtration that exhibited the strongest ACE inhibitory activity was chromatographed by reversed-phase HPLC, each fraction was individually collected, and the amino acid sequence was determined by a protein sequencer. We found four ACE inhibitory peptides (Gly-Tyr, Ala-Tyr, Val-Tyr, and Gly-Phe) in mirin.
日本調理科学会の論文
2005-10-20