| Literature DB >> 34366467 |
Wen-Ying Liu1,2,3, Takuya Miyakawa3, Jun Lu2, Yun Hua Hsieh3, Ruizeng Gu2, Yumiko Miyauchi3, Kana Katsuno3, Mu-Yi Cai2, Masaru Tanokura3.
Abstract
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. © Association of Food Scientists & Technologists (India) 2021.Entities:
Keywords: Antithrombotic activity; Cholesterol reducing activity; Vasorelaxation activity; Wheat oligopeptides
Year: 2021 PMID: 34366467 PMCID: PMC8292472 DOI: 10.1007/s13197-021-05040-5
Source DB: PubMed Journal: J Food Sci Technol ISSN: 0022-1155 Impact factor: 3.117