ArticleUltrasonics sonochemistry2026
Sonication integrated with micronization: structural modification to improve the in-vitro digestibility, functional, and antioxidant properties of red pepper seed protein isolate.
Article in Ultrasonics sonochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The study aimed to extract protein from red pepper seeds and to probe the effects of micronization (MN) at 15,000 rpm for 3 and 6 min, ultrasound (US) at 720 W, 40 kHz for 10 and 15 min, and their combined impact on red pepper seed protein isolate (RPSPI). The combined treatment (MN 6 min and US 10 min) substantially reduced particle size and increased -ve zeta potential, thereby significantly increasing RPSPI stability compared to untreated and individual treatments. Structural results showed significant molecular changes: increased free-SH content and surface hydrophobicity, and decreased intrinsic fluorescence intensity, indicating improved exposure of buried residues and partial unfolding. Fourier Transform Infrared peak spectra results verified secondary structural modification, evidenced by a significant increase in random coil and α-helix content. The disruption and significant fragmentation observed in Scanning Electron Microscope micrographs confirmed these findings. Thermograms from Differential Scanning Calorimetry and X-ray diffraction patterns showed decreases in the thermal transition temperature and crystallinity, respectively, indicating weak intermolecular interactions. These structural changes in RPSPI significantly increased the water solubility, emulsifying activity, foaming capacity, and water and oil holding capacity, while decreasing the turbidity. Also, combined treatment significantly enhanced the ABTS, DPPH, and OH scavenging abilities (%) of RPSPI and in vitro protein digestibility. Conclusively, results revealed that this extremely underexploited by-product protein can develop into a value-added ingredient by improving its techno-functional and bioactive properties through these non-thermal technologies.
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.