Evidence map›Paper›PMID 35106485›Full record

ArticleCurrent research in food science2022

Mitigation of antinutritional factors and protease inhibitors of defatted winged bean-seed proteins using thermal and hydrothermal treatments: Denaturation/unfolding coupled hydrolysis mechanism.

Sami Saadi, Nazamid Saari, Hasanah Mohd Ghazali, Mohammed Sabo Abdulkarim

Abstract read
In one paragraph

Article in Current research in food science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Isolation and evaluation of quinoa (Current research in food science · 2022
    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

4 authors.

Sami SaadiInstitut de la Nutrition, de l'Alimentation et des Technologies Agro-alimentaires INATAA 25017, Université Frères Mentouri, Constantine 1, Algeria.
Nazamid SaariDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia.
Hasanah Mohd GhazaliDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia.
Mohammed Sabo AbdulkarimDepartment of Microbiology and Biotechnology, Federal University Dutse, Nigeria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inactivation of antinutritional factors, protease inhibitors within winged bean protein was induced by two respective method treatments. The physical method based on steam vapor that was conducted using an autoclave and chemical method consisting on pH-gradients of buffer solutions prepared at respective acidic pH, neutral pH and alkaline pH ranges. The activity of remaining protease inhibitors of bowman birk inhibitor (BBI), and kunitz-trypsin inhibitor (KTI) after and before treatments was enzymatically confirmed using relevant antagonistic trypsin and combined trypsin-α-chymotrypsin digests. The resulting molecular assembly indicating an interval molecular relaxation range of °0.16 < °DA < °0.2 corresponding to reconformation in protein units with volume-mass changes of -2.17 < ∂v' < +2.17 and with denaturation/unfolding efficiency based on heat capacity ΔCp of 36.36 < DE/UF% < 54.67. These structural changes had a great benefit in determining and producing functional protein hydrolysates.

Indexed as

Competitive inhibitorsDenaturation/unfoldingHydrolysis levelsMolecular assemblyProteolysatesTransition energy

Identifiers

PMID35106485
PMCPMC8789533

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.