Evidence map›Paper›PMID 36825069›Full record

ArticleFrontiers in nutrition2022

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf.

Yu Chen, Yu Zhang, Qianhui Qi, Feng Liang, Nan Wang, Qihe Chen, Xue Li, Suling Sun, Xinquan Wang, Kaiwen Bai and 2 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in nutrition, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 14 citations in OpenAlex.

  1. Pooled it
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  12. Development of Data Mining Algorithms for Identifying the Best Anthropometric Predictors for Cardiovascular Disease: MASHAD Cohort Study.High blood pressure & cardiovascular prevention : the official journal of the Italian Society of Hypertension · 2023
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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

12 authors at 7 institutions in 1 country.

Yu ChenCollege of Agriculture and Animal Husbandry, Qinghai University, Xining, China.
Yu ZhangInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Qianhui QiInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Feng LiangInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Nan WangZhejiang Shuren University, Hangzhou, China.
Qihe ChenSchool of Biological Systems Engineering and Food Science, Zhejiang University, Hangzhou, China.
Xue LiInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Suling SunInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Xinquan WangInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Kaiwen BaiSchool of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou, China.
Wei WangInstitute of Agricultural Safety and Nutrition, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Yingchun JiaoCollege of Agriculture and Animal Husbandry, Qinghai University, Xining, China.
ZheJiang Academy of Agricultural Sciences · CNBohai University · CNMinistry of Agriculture and Rural Affairs · CNQinghai University · CNZhejiang Shuren University · CNZhejiang University · CNZhejiang University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiotensin-I converting enzyme (ACE) inhibitory peptides drew wide attention in the food industry because of their natural reliability, non-toxicity, and safety. However, the characteristics of ACE inhibitory peptides obtained from protein hydrolysate of mulberry leaf prepared by Flavourzyme were still unclear. Based on the single-factor test, the Plackett-Burman test and response surface test were used to determine the key factors affecting the ACE inhibition rate in mulberry leaf protein hydrolysate and the optimum conditions of enzymatic hydrolysis. The results showed that the optimum technical parameters were as follows: the ratio of material to liquid is 1: 25 (w / v, g/mL), the Flavourzyme to substrate ratio was 3,000 U/g, the temperature of enzymatic hydrolysis was 50°C, pH was 6.3, and the time of enzymatic hydrolysis was 2.9 h. The ACE inhibitory peptides in the mulberry leaf protein hydrolysates were purified by ultrafiltration and gel filtration, aiming to obtain the highest active component. The 12 peptide sequences were identified by reverse liquid chromatography-mass spectrometry, and then, they were docked to the crystal structure of human angiotensin-I converting enzyme (1O8A), and the interaction mechanisms of 12 peptide sequences and 1O8A were analyzed. The docking results showed that among the 12 peptide sequences, ERFNVE (792.37 Da), TELVLK (351.72 Da), MELVLK (366.72 Da), and FDDKLD (376.67 Da), all had the lowest docking energy, and inhibition constant. The chemosynthetic ERFNVE (IC

Indexed as

angiotensin-I converting enzyme (ACE)hydrolysateinhibitory peptidesmolecular dockingmulberry leaf protein

Identifiers

PMID36825069
PMCPMC9941179
OpenAlexW4319443996

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.