Evidence map›Paper›PMID 41373494›Full record

ArticleInternational journal of molecular sciences2025

Protein-Dependent, pH-Selective Complexation in Tragacanth-Protein Systems: An Integrated FTIR-DLS-Rheology-Docking Study.

Jagoda O Szafrańska

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Jagoda O SzafrańskaDepartment of Dairy Technology and Functional Food, Faculty of Food Sciences and Biotechnology, University of Life Sciences, Skromna 8, 20-704 Lublin, Poland.ORCID 0000-0002-4178-0504

Funding

University of Life Sciences in Lublin VKZ/MN-15/TŻ/2023-25
6 · The paper itself

Abstract

Tragacanth gum (GT) was mixed with whey protein concentrate (WPC80), whey protein isolate (WPI) or rice protein (RP) across pH 3.0-7.2 in order to clarify the effect of protein type and pH on controlling association and bulk behavior. Turbidimetry at 600 nm by photographic validation, oscillatory and steady-shear rheology, dynamic light scattering (DLS), FTIR spectroscopy, and AutoDock Vina docking were employed and compared. Whey systems reflected a clear, mildly acidic window: low-strain elasticity (G') reached near pH ~5, with increased A600 and dominant sub-100 nm DLS modes, reflecting associative complexation near the isoelectric region. WPI also reflected a secondary turbidity/viscosity rise at pH 7.2, consistent with segregative aggregationafter the associative window. RP was variable, featuring broadly increased turbidity with viscosity/DLS maxima at pH 6.4, reflecting glutelin-facilitated solubility/aggregation rather than an acid optimum. FTIR changes in the amide band and GT bands (COO

Indexed as

Plant ProteinsTragacanthWhey ProteinsDynamic Light ScatteringHydrogen-Ion ConcentrationMolecular Docking SimulationRheologySpectroscopy, Fourier Transform InfraredViscosityPlant ProteinsTragacanthWhey ProteinsDLSFTIRmolecular dockingpH-dependent complexationprotein–polysaccharide complexesrheologytragacanth gum

Identifiers

PMID41373494
PMCPMC12692447

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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.