ArticlePloS one2025
Fluorometric combination analysis of conformational changes in urea-induced unfolding of soybean protein isolates and their complexes with casein.
Article in PloS one, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soybean proteins isolates (SPIs) could misfold to form amorphous aggregates after unfolding due to processing conditions, leading to a decrease in their solubility, and casein might be able to block the formation of amorphous aggregates. The turbidity curves showed that SPIs/7S/11S could maintain a soluble state in the presence of casein. The folding and unfolding processes of SPIs are not a single-step event. Fluorescence phase diagram method was utilized to analyze the unfolding process of SPIs and SPI-casein complexes. The results showed that there was one intermediate (molten globule, MG) in the unfolding process of SPIs, while there were two intermediates (dimer or trimer intermediates and MG) in that of SPI-casein complexes. Further attempts were made to explain the conformational changes of SPIs when binding with casein. The surface hydrophobicity index indicated that the intermediate with strong hydrophobicity was exposed when induced by 2 mol/L urea. The fluorescence quenching experiments using KI as a quencher showed that the Ksv of SPIs and 11S and their complexes with casein all reached peak values when urea concentration was 2 mol/L, while Ksv values of 7S and 7S-casein complex peaked at urea concentration 8mol/L and 6mol/L, respectively. Besides, Ksv and fm changing trends of 7S-casein complex was similar to that of SPIs-casein. Based on the above results, it could be inferred that the interactions between SPIs and casein mainly occurs in 7S. The molecular docking of 7S chains from SPIs and casein showed that SPIs could form a "pocket" conformation to "hold" the casein chain. These findings provide new perspectives for understanding the mechanism of interaction between soy proteins and casein, and may provide a basis for research on the functionality of proteins in the food industry. Note: Ksv is the quenching constant of the quenching agent, and fm is the quenching rate.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.