Evidence map›Paper›PMID 38904703›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2024

Understanding Stabilization of Oil-in-Water Emulsions with Pea Protein─Studies of Structure and Properties.

Eleonora Olsmats, Adrian R Rennie

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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

2 authors.

Eleonora OlsmatsMacromolecular Chemistry, Department of Chemistry─Ångström, Uppsala University, Box 538, 75121 Uppsala, Sweden.ORCID 0009-0003-8175-2158
Adrian R RennieMacromolecular Chemistry, Department of Chemistry─Ångström, Uppsala University, Box 538, 75121 Uppsala, Sweden.ORCID 0000-0001-8185-3272

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study investigates the stability and structure of oil-in-water emulsions stabilized by pea protein. Of the wide range of emulsion compositions explored, a region of stability at a minimum of 5% w/v pea protein and 30-50% v/v oil was determined. This pea protein concentration is more than what is needed to form a layer covering the interface. X-ray scattering revealed a thick, dense protein layer at the interface as well as hydrated protein dispersed in the continuous phase. Shear-thinning behavior was observed, and the high viscosity in combination with the thick protein layer at the interface creates a good stability against creaming and coalescence. Emulsions in a pH range from acidic to neutral were studied, and the overall stability was observed to be broadly similar independently of pH. Size measurements revealed polydisperse protein particles. The emulsion droplets are also very polydisperse. Apart from understanding pea protein-stabilized emulsions in particular, insights are gained about protein stabilization in general. Knowledge of the location and the role of the different components in the pea protein material suggests that properties such as viscosity and stability can be tailored for various applications, including food and nutraceutical products.

Indexed as

EmulsionsOilsPea ProteinsWaterHydrogen-Ion ConcentrationParticle SizePisum sativumViscosityEmulsionsOilsPea ProteinsWater

Identifiers

PMID38904703
PMCPMC11223488

What OpenQuestion holds

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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.