ArticleFoods (Basel, Switzerland)2025
Effects of Ultrasonic-Assisted Enzymatic Treatment on the Solubility and Stability of Myofibrillar Protein from Tilapia (
Article in Foods (Basel, Switzerland), 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
6 authors.
Funding
Abstract
Myofibrillar protein (MP) aggregation in solutions with NaCl concentrations below 0.3 M results in poor solubility. Ultrasound-assisted glutaminase treatment (UGT) was applied to improve MP solubility in a low-salt solution (containing 0.1 M NaCl). The solubility increased with ultrasonic power and time, peaking at 44.34% (480 W, 15 min) and reaching 61% after UGT. Subsequently, the effect of post-sonication heat treatment (60 °C, 30 min) on the physicochemical and structural characteristics of ultrasound-enzyme treated MP (UEMP), prepared under specific ultrasonic conditions (480 W, 20 min), was systematically investigated. The findings revealed that UEMP exhibited higher hydrophobicity, sulfhydryl content, and turbidity, but reduced particle size, ζ-potential, and fluorescence, suggesting disulfide disruption and exposure of hydrophobic residues. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed weakened high-molecular weight bands and intensified low-molecular weight bands. Fourier-transform infrared spectroscopy confirmed these structural rearrangements, with a blue-shifted amide A band and decreased amide I intensity. Heating further increased the hydrophobicity and fluorescence without altering the size, ζ-potential, or molecular weight. The red shift in the amide A band suggests reinforced local ordering. Rheology analysis showed non-Newtonian shear-thinning behavior, which was unchanged by UGT or heating. Collectively, UGT with moderate heating enhances MP solubility and thermal stability by disrupting stabilizing bonds and modulating the structure.
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.