Evidence map›Paper›PMID 34366467›Full record

ArticleJournal of food science and technology2021

Isolation and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten.

Wen-Ying Liu, Takuya Miyakawa, Jun Lu, Yun Hua Hsieh, Ruizeng Gu, Yumiko Miyauchi, Kana Katsuno, Mu-Yi Cai, Masaru Tanokura

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of food science and technology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed, 1 pooled it
0.4field-weighted citation impact, top 42% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 synthesis or guideline pooled it, 7 citations in OpenAlex.

  1. Pooled it
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Wen-Ying LiuCollege of Engineering, China Agricultural University, Beijing, 100083 People's Republic of China.ORCID 0000-0001-8369-0809
Takuya MiyakawaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657 Japan.
Jun LuBeijing Engineering Research Center of Functional Peptides, China National Research Institute of Food and Fermentation Industries Co. Ltd., Beijing, 100015 People's Republic of China.
Yun Hua HsiehDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657 Japan.
Ruizeng GuBeijing Engineering Research Center of Functional Peptides, China National Research Institute of Food and Fermentation Industries Co. Ltd., Beijing, 100015 People's Republic of China.
Yumiko MiyauchiDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657 Japan.
Kana KatsunoDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657 Japan.
Mu-Yi CaiBeijing Engineering Research Center of Functional Peptides, China National Research Institute of Food and Fermentation Industries Co. Ltd., Beijing, 100015 People's Republic of China.
Masaru TanokuraDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657 Japan.
The University of Tokyo · JPChina National Research Institute of Food and Fermentation · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Antithrombotic activityCholesterol reducing activityVasorelaxation activityWheat oligopeptides

Identifiers

PMID34366467
PMCPMC8292472
OpenAlexW3129550598

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.