Evidence map›Paper›PMID 34473745›Full record

ArticlePloS one2021

A novel angiotensin I-converting enzyme inhibitory peptide derived from the trypsin hydrolysates of salmon bone proteins.

Thanakrit Kaewsahnguan, Sajee Noitang, Papassara Sangtanoo, Piroonporn Srimongkol, Tanatorn Saisavoey, Onrapak Reamtong, Kiattawee Choowongkomon, Aphichart Karnchanatat

Abstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

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

  1. Pooled it
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  3. Circular Valorization of Yellowfin Tuna (Molecules (Basel, Switzerland) · 2026
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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.

Thanakrit KaewsahnguanProgram in Biotechnology, Faculty of Science, Chulalongkorn University, Pathumwan, Bangkok, Thailand.
Sajee NoitangResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, Pathumwan, Bangkok, Thailand.ORCID 0000-0002-7838-2366
Papassara SangtanooResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, Pathumwan, Bangkok, Thailand.
Piroonporn SrimongkolResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, Pathumwan, Bangkok, Thailand.
Tanatorn SaisavoeyResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, Pathumwan, Bangkok, Thailand.
Onrapak ReamtongDepartment of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, Thailand.
Kiattawee ChoowongkomonDepartment of Biochemistry, Faculty of Science, Kasetsart University, Chatuchak, Bangkok, Thailand.
Aphichart KarnchanatatResearch Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, Pathumwan, Bangkok, Thailand.ORCID 0000-0002-6598-013X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When fish are processed, fish bone becomes a key component of the waste, but to date very few researchers have sought to use fish bone to prepare protein hydrolysates as a means of adding value to the final product. This study, therefore, examines the potential of salmon bone, through an analysis of the benefits of its constituent components, namely fat, moisture, protein, and ash. In particular, the study seeks to optimize the process of enzymatic hydrolysis of salmon bone with trypsin in order to produce angiotensin-I converting enzyme (ACE) inhibitory peptides making use of response surface methodology in combination with central composite design (CCD). Optimum hydrolysis conditions concerning DH (degree of hydrolysis) and ACE-inhibitory activity were initially determined using the response surface model. Having thus determined which of the salmon bone protein hydrolysates (SBPH) offered the greatest level of ACE-inhibitory activity, these SBPH were duly selected to undergo ultrafiltration for further fractionation. It was found that the greatest ACE-inhibitory activity was achieved by the SBPH fraction which had a molecular weight lower than 0.65 kDa. This fraction underwent further purification using RP-HPLC, revealing that the F7 fraction offered the best ACE-inhibitory activity. For ACE inhibition, the ideal peptide in the context of the F7 fraction comprised eight amino acids: Phe-Cys-Leu-Tyr-Glu-Leu-Ala-Arg (FCLYELAR), while analysis of the Lineweaver-Burk plot revealed that the FCLYELAR peptide can serve as an uncompetitive ACE inhibitor. An examination of the molecular docking process showed that the FCLYELAR peptide was primarily able to provide ACE-inhibitory qualities as a consequence of the hydrogen bond interactions taking place between ACE and the peptide. Furthermore, upon isolation form the SBPH, the ACE-inhibitory peptide demonstrated ACE-inhibitory capabilities in vitro, underlining its potential for applications in the food and pharmaceutical sectors.

Indexed as

Amino Acid SequenceAngiotensin-Converting Enzyme InhibitorsAnimalsBinding SitesBone and BonesFactor Analysis, StatisticalHydrogen BondingHydrolysisKineticsModels, MolecularMolecular Docking SimulationMolecular WeightPeptidyl-Dipeptidase AProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandACE protein, humanAngiotensin-Converting Enzyme InhibitorsPeptidyl-Dipeptidase AProtein HydrolysatesTrypsin

Identifiers

PMID34473745
PMCPMC8412326

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.