Evidence map›Paper›PMID 37081859›Full record

ArticleCurrent research in food science2023

High pressure homogenization to boost the technological functionality of native pea proteins.

Giulia D'Alessio, Federica Flamminii, Marco Faieta, Roberta Prete, Alessandro Di Michele, Paola Pittia, Carla Daniela Di Mattia

Open access · goldAbstract read
In one paragraph

Article in Current research in food science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
9.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Rethinking Plant Proteins: Innovations in Nutrition, Processing, and Food Development.Plant foods for human nutrition (Dordrecht, Netherlands) · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Pea Protein Isolates: From Extraction to Functionality.Molecules (Basel, Switzerland) · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Ultrasound-Assisted Enzymatic Extraction ofFood science & nutrition · 2025
    Article
  15. Article
  16. Peas (Molecules (Basel, Switzerland) · 2025
    Review
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Giulia D'AlessioDepartment of Bioscience and Agro-Food and Environmental Technology, University of Teramo, Via R. Balzarini 1, 64100, Teramo, Italy.
Federica FlamminiiDepartment of Innovative Technologies in Medicine and Dentistry, University "G. D'Annunzio" of Chieti-Pescara, Via dei Vestini, 66100, Chieti, Italy.
Marco FaietaDepartment of Bioscience and Agro-Food and Environmental Technology, University of Teramo, Via R. Balzarini 1, 64100, Teramo, Italy.
Roberta PreteDepartment of Bioscience and Agro-Food and Environmental Technology, University of Teramo, Via R. Balzarini 1, 64100, Teramo, Italy.
Alessandro Di MicheleDepartment of Physics and Geology, University of Perugia, Via Pascoli, 06123, Perugia, Italy.
Paola PittiaDepartment of Bioscience and Agro-Food and Environmental Technology, University of Teramo, Via R. Balzarini 1, 64100, Teramo, Italy.
Carla Daniela Di MattiaDepartment of Bioscience and Agro-Food and Environmental Technology, University of Teramo, Via R. Balzarini 1, 64100, Teramo, Italy.
University of Teramo · ITUniversity of Chieti-Pescara · ITUniversity of Perugia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pea proteins are being increasingly used for the formulation of plant-based products, but their globular structure and the presence of aggregates can affect their technological properties. In this study, the effect of high pressure homogenization (HPH) at different intensities (60 and 100 MPa) was investigated as a pre-treatment to modulate the techno-functional properties of a pea protein isolate (IP) extracted through an alkaline extraction/isoelectric precipitation process. SDS-PAGE, circular dichroism, thermal properties, total free sulfhydryl groups, antioxidant capacity and reducing properties were evaluated along with technological indices as solubility, WHC and OHC, interfacial tension and emulsifying capacity. HPH treatments were able to unfold and modify proteins structure, leading also to a change of the relative abundance of pea protein globulins (SDS-PAGE) and of the vicilin to legumin ratio. Solubility, WHC and OHC were improved, while interfacial tension and emulsifying capacity were weakly affected. However, an enhanced physical stability over time of the emulsions prepared with the 60 MPa-treated protein was found, likely as an effect of the decreased ratio between vicilin and legumin after treatment. Results of this study will contribute to deepen the effect of the HPH technology used as pre-treatment, adding useful results and expanding knowledge about the structure and techno-functional properties of native and modified pea proteins.

Indexed as

EmulsionsHigh pressure homogenizationPea proteinsSolubilityTechnological properties

Identifiers

PMID37081859
PMCPMC10111953
OpenAlexW4361287999

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.