Evidence map›Paper›PMID 42137117›Full record

ArticleJournal of food process engineering2025

Small angle X-ray scattering studies on the effects of ultra shear technology on model animal and plant-based protein solutions.

Jerish Joyner Janahar, Hetian Hu, V M Balasubramaniam, Susana C M Teixeira

Abstract read
In one paragraph

Article in Journal of food process engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Review
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

4 authors.

Jerish Joyner JanaharDepartment of Food Science and Technology, The Ohio State University, Columbus, Ohio, USA.
Hetian HuDepartment of Food Agricultural and Biological Engineering, The Ohio State University, Columbus, Ohio, USA.
V M BalasubramaniamDepartment of Food Science and Technology, The Ohio State University, Columbus, Ohio, USA.ORCID 0000-0002-1540-4273
Susana C M TeixeiraDepartment of Chemical and Biomolecular Engineering, University of Delaware, Delaware, USA.ORCID 0000-0002-6603-7936

Funding

The Biophysics Collaborative Access Team (User Training and Outreach)P30GM138395 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI THOMAS C IRVING · 2021 to 2026
$16.5M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Intramural NIST DOC 9999-NISTNIGMS NIH HHS P30 GM138395NIGMS NIH HHS R01 GM129325
6 · The paper itself

Abstract

The effects of shear, temperature and high pressure on model solutions of bovine milk and plant proteins were investigated. Samples of bovine β-lactoglobulin (BLG), pea lectin (PL), and their mixture (MIX), were treated by high-pressure processing (HPP) and ultra-shear technology (UST). BLG and PL are known for their allergenic properties, and processing conditions can potentially be used to decrease allergenicity, as well as engineer beverage properties of interest. Small angle X-ray scattering (SAXS) and confocal laser scanning microscopy (CLSM) were used to measure the impact of processing on the protein solutions from the microscopic to the molecular scale. SAXS data were analyzed by various approaches, to assess changes in protein size and shape, oligomerization and aggregation. The results are consistent with the BLG sensitivity to shear, pressure and temperature, where the pressure holding time was shown to be critical and thermal effects at ambient pressure are distinct from those observed under pressure. Although some changes in shape were detected, PL showed structural and colloidal resistance to the processing conditions applied. The MIX solutions appear to show a convolution of the effects observed on the isolated protein solutions, granting further investigation to clarify potential interactions between the proteins. These findings are valuable for the development of liquid protein foods based on animal and plant proteins and their blends, enhancing control over functional properties and expanding their applications in food, nutraceuticals, and biomedical fields.

Indexed as

beta–-lactoglobulinhigh-pressure processingpea lectinplant proteinssmall angle scatteringUltra shear technology

Identifiers

PMID42137117
PMCPMC13170502

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Registered trials

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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.