Evidence map›Paper›PMID 40896659›Full record

ArticleFood chemistry: X2025

Thermal denaturation of porcine myofibrillar proteins at different heating temperatures: A focus on the surface hydrophobicity.

Seonmin Lee, Kyung Jo, Soeun Kim, Seokhee Han, Samooel Jung

Abstract read
In one paragraph

Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Review
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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

5 authors.

Seonmin LeeResearch Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of Korea.
Kyung JoDepartment of Animal Science and Biotechnology, Chungnam National University, Daejeon 34134, Republic of Korea.
Soeun KimDepartment of Animal Science and Biotechnology, Chungnam National University, Daejeon 34134, Republic of Korea.
Seokhee HanDepartment of Animal Science and Biotechnology, Chungnam National University, Daejeon 34134, Republic of Korea.
Samooel JungDepartment of Animal Science and Biotechnology, Chungnam National University, Daejeon 34134, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Changes in the hydrophobic interactions of porcine myofibrillar proteins (MPs) were investigated at various heating and internal temperatures (ITs). MP extracts were heated at 50, 60, 70, 80, or 90 °C until their ITs reached the same respective values (±2 °C) and were labeled IT50, IT60, IT70, IT80, and IT90. The intrinsic tryptophan fluorescence intensity (FI) of the MPs decreased after heating at all ITs (

Indexed as

Circular dichroism spectroscopyMyofibrillar proteinSurface hydrophobicityThermal denaturationTryptophan fluorescence intensity

Identifiers

PMID40896659
PMCPMC12391829

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.