Evidence map›Paper›PMID 34201554›Full record

SynthesisMolecules (Basel, Switzerland)2021

Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review.

Azis Boing Sitanggang, Jessica Eka Putri, Nurheni Sri Palupi, Emmanuel Hatzakis, Elvira Syamsir, Slamet Budijanto

Open access · goldAbstract readSystematic Review
In one paragraph

Synthesis in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Step Enzymatic Hydrolysis andFoods (Basel, Switzerland) · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Frontiers in physiology · 2023
    Article
  10. Article
  11. Article
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

6 authors at 2 institutions in 2 countries.

Azis Boing SitanggangDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia.ORCID 0000-0002-1378-5367
Jessica Eka PutriDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia.
Nurheni Sri PalupiDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia.
Emmanuel HatzakisDepartment of Food Science and Technology, The Ohio State University, 2015 Fyffe Rd, Columbus, OH 43210, USA.
Elvira SyamsirDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia.
Slamet BudijantoDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia.
IPB University · IDThe Ohio State University · US

Funding

Kementerian Riset Teknologi Dan Pendidikan Tinggi Republik Indonesia WCR Program 2325 /IT3.L1/PN/2021.
6 · The paper itself

Abstract

The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from

Indexed as

Amino AcidsAngiotensin-Converting Enzyme InhibitorsAspergillusEndopeptidasesExopeptidasesGlobulinsGlycine maxHydrolysisHydrophobic and Hydrophilic InteractionsMucunaPancreatinPeptide HydrolasesPeptidesProlineSoybean ProteinsTemperatureAmino AcidsAngiotensin-Converting Enzyme InhibitorsEndopeptidasesExopeptidasesGlobulinsglycininPancreatinPeptide HydrolasesPeptidesProlineSoybean Proteinsangiotensin-I-converting enzyme (ACE)bioactive peptideendopeptidaseenzymatic hydrolysisexopeptidasesoybeanvelvet bean

Identifiers

PMID34201554
PMCPMC8270263
OpenAlexW3174222234

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.