Open AccessIsolation and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten
Author(s) -
Wenying Liu,
Takuya Miyakawa,
Jun Lu,
Yun Hua Hsieh,
Rong Gu,
Yumiko Miyauchi,
Kana Katsuno,
Mingyue Cai,
Masaru Tanokura
Publication year - 2021
Publication title -
journal of food science and technology/journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.656
H-Index - 68
eISSN - 0975-8402
pISSN - 0022-1155
DOI - 10.1007/s13197-021-05040-5
Subject(s) - neutral protease , oligopeptide , wheat gluten , chemistry , antithrombotic , gluten , protease , peptide , chromatography , biochemistry , enzyme , medicine
Wheat gluten was hydrolyzed with both alkaline protease and neutral protease to produce high-protein and low-wheat-weight oligopeptides (WOP), which was subjected to a multistage purification. Then, high performance liquid chromatography was applied to separate WOP. In order to identify WOP sequences, six major fractions were gathered for mass spectrometry. A total of 15 peptides were synthesized for further in vitro analyses of their antithrombotic activity, vasorelaxation activity, and cholesterol reducing activity. Two antithrombotic peptides (ILPR and ILR), three vasorelaxant peptides (VN, FPQ, and FR), and four cholesterol-lowering peptides (QRQ, ILPR, FPQ, and ILR) were identified. These active peptides in WOP were also quantified. These peptides are novel candidate peptides with vascular disease suppressing effects. The results indicate WOP as good protein sources for multifunctional peptides.