ArticleJournal of the science of food and agriculture2026
Tailoring whey protein isolate properties through controlled cold plasma processing: excitation frequency, voltage and time as key variables.
Article in Journal of the science of food and agriculture, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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
2 citing papers in PubMed.
- Role of Non-Thermal Processing Technologies in Modulating Protein Allergenicity in Legumes.Food science & nutrition · 2026Review
- Mild thermal unfolding of pea protein enhances curcumin binding and interfacial properties of the resulting complexes.Food chemistry: X · 2026Article
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
Abstract
backgroundCold plasma (CP) is a promising nonthermal technology for tailoring protein structure and functionality. Its ability to induce conformational rearrangements makes it a potential tool for improving the techno-functional performance of whey protein isolate (WPI). WPI was subjected to CP treatment under varying frequencies (50, 500 and 950 Hz), voltages (10, 15 and 20 kV) and times (10, 15 and 20 min). Analyses included secondary structure (Fourier transform infrared), zeta potential, surface hydrophobicity, carbonyl and free sulfhydryl contents, solubility and curcumin-protein fluorescence binding parameters.
resultsCP increased α-helix and β-sheet contents, promoting protein aggregation. Zeta potential was positively affected by higher frequency but reduced by higher voltage. Surface hydrophobicity consistently increased, while free sulfhydryl content decreased with frequency but increased with time and voltage. Carbonyl content rose under stronger treatments. Solubility decreased across all conditions, attributed to aggregation. Binding affinity (K
conclusionsControlled CP treatment significantly modified WPI structure and functional behavior, reducing solubility and binding affinity while enhancing aggregation. These findings demonstrate the potential of CP as a versatile tool to tailor protein properties for food applications. © 2025 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.
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.