Evidence map›Paper›PMID 35492113›Full record

ArticleRSC advances2020

Two novel ACE inhibitory peptides isolated from longan seeds: purification, inhibitory kinetics and mechanisms.

Atthasith Nuchprapha, Supawee Paisansak, Papassara Sangtanoo, Piroonporn Srimongkol, Tanatorn Saisavoey, Onrapak Reamtong, Kiattawee Choowongkomon, Aphichart Karnchanatat

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 51 citations in OpenAlex.

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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

8 authors at 3 institutions in 4 countries.

Atthasith NuchpraphaProgram in Biotechnology, Faculty of Science, Chulalongkorn University 254 Phayathai Road, Pathumwan Bangkok 10330 Thailand.
Supawee PaisansakProgram in Biotechnology, Faculty of Science, Chulalongkorn University 254 Phayathai Road, Pathumwan Bangkok 10330 Thailand.
Papassara SangtanooResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University 254 Phayathai Road, Pathumwan Bangkok 10330 Thailand Aphichart.K@chula.ac.th.
Piroonporn SrimongkolResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University 254 Phayathai Road, Pathumwan Bangkok 10330 Thailand Aphichart.K@chula.ac.th.
Tanatorn SaisavoeyResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University 254 Phayathai Road, Pathumwan Bangkok 10330 Thailand Aphichart.K@chula.ac.th.
Onrapak ReamtongDepartment of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University 420/6 Ratchawithi Road, Ratchathewi Bangkok 10400 Thailand.
Kiattawee ChoowongkomonDepartment of Biochemistry, Faculty of Science, Kasetsart University Bangkok 10903 Thailand.
Aphichart KarnchanatatResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University 254 Phayathai Road, Pathumwan Bangkok 10330 Thailand Aphichart.K@chula.ac.th.ORCID https://orcid.org/0000-0002-6598-013X
Chulalongkorn University · THKasetsart University · THMahidol University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiotensin converting enzyme (ACE) inhibition offers a useful means of managing hypertension, because ACE inhibitors (ACEIs) are known to serve as agents with antihypertensive properties in addition to generating positive metabolic and cardioprotective outcomes. However, current ACEIs are linked to adverse consequences, and so there is a requirement for effective but safer compounds, which might be achieved through chemical synthesis or the isolation of naturally obtained bioactive molecules. Protein hydrolysates with ACEI activity can be produced by the combined pepsin and pancreatin proteolysis (to mimic gastrointestinal digestion) of longan seed protein. This study examined longan seed protein hydrolysates, obtained from a sequential 3 h digestion with pepsin and then pancreatin. The resulting hydrolysate underwent sequential ultrafiltration membrane fractionation with a 10, 5, and 3 kDa molecular weight cut-off (MWCO). The permeate derived from the <3 kDa MWCO demonstrated the highest ACEI activity. This permeate subsequently underwent separation by reverse-phase high performance liquid chromatography to give the main fractions on the basis of differing elution times. The ACEI IC

Identifiers

PMID35492113
PMCPMC9051311
OpenAlexW3013929207

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.