ArticleFood chemistry: X2022
Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study.
Article in Food chemistry: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 14 citations in OpenAlex.
- Physicochemical, Textural, and Rheological Properties of Bigels Prepared from Large Yellow Croaker Myofibrillar Proteins and κ-Carrageenan.Foods (Basel, Switzerland) · 2026Article
- Protein-Dependent, pH-Selective Complexation in Tragacanth-Protein Systems: An Integrated FTIR-DLS-Rheology-Docking Study.International journal of molecular sciences · 2025Article
- Microencapsulation ofJournal of food science and technology · 2023Article
- Effect of Adding Different Commercial Propylene Glycol Alginates on the Properties of Mealworm-Flour-Formulated Bread and Steamed Bread.Foods (Basel, Switzerland) · 2023Article
- Emulsion Properties during Microencapsulation of Cannabis Oil Based on Protein and Sucrose Esters as Emulsifiers: Stability and Rheological Behavior.Foods (Basel, Switzerland) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interactions between whey protein isolate (WPI) and propylene glycol alginate (PGA) were investigated as a function of pH and the mass ratio. The results showed that WPI and PGA formed a soluble and uniform complex at a mass ratio of 2:1 and pH 4.0 through forces such as electrostatic attraction and hydrogen bonding. Isothermal titration calorimetry confirmed that the contribution of positive enthalpy (ΔH) and entropy (ΔS) were the beneficial indicator in the process of combining WPI and PGA under the same mass ratio but different pH. Fourier transform infrared spectroscopy, fluorescence spectroscopy and circular dichroism confirmed that hydrogen bonding was also one of the interaction forces in addition to electrostatic interactions between WPI-PGA complex. The freeze-dried WPI-PGA complex showed the same amorphous structure as WPI. These formed WPI-PGA complexes provided insights for interaction mechanism of proteins and polysaccharides as well as a theoretical basis for the food 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.