Evidence map›Paper›PMID 38201204›Full record

ArticleFoods (Basel, Switzerland)2024

Physicochemical Quantitative Analysis of the Oil-Water Interface as Affected by the Mutual Interactions between Pea Protein Isolate and Mono- and Diglycerides.

Ziyan Wang, Jingwen Li, Chao Peng, Bin Li, Qian Shen, Yijie Chen

Open access · goldAbstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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

6 authors at 4 institutions in 2 countries.

Ziyan WangHubei Key Laboratory for Processing and Transformation of Agricultural Products and College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China.
Jingwen LiNational Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China.
Chao PengNational Facility for Protein Science in Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China.ORCID 0000-0002-6814-2676
Bin LiCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
Qian ShenHubei Key Laboratory for Processing and Transformation of Agricultural Products and College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China.
Yijie ChenCollege of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
Chinese Academy of Sciences · CNHuazhong Agricultural University · CNUniversity of Leeds · GBWuhan Polytechnic University · CN

Funding

Fundamental Research Funds for the Central Universities 2662023PPY003Hubei Key R&D Program 2023BBB130National Natural Science Foundation of China 31972019Open Fund of Key Laboratory of Fermentation Engineering (Ministry of Education) 202209FE01the National Key R&D Program of China 2022YFD2101302
6 · The paper itself

Abstract

As a commercially available ingredient, the mono- and diglycerides (MDG) were widely used in a plant protein-based emulsion to provide effective, functional, emulsifying properties. The simultaneous addition of the MDG and pea protein isolate (PPI) was investigated by the methods of interfacial rheology and quantitative protein proteomics. The physicochemical quantitative analysis of the oil-water interface revealed an interfacial stability mechanism for the protein adsorption layer. For a low MDG concentration, the interfacial quantities of vicilin and albumin were increased, which could be attributed to the adsorption rate. For a high MDG concentration, both vicilin and albumin were displaced by MDG and desorbed from the interface, while legumin was more difficult to displace due to its slow adsorption and the complex structure of protein molecules. The protein molecules with the structural rearrangement interacted with MDG, exhibiting potential effects on the interfacial film structure. Combined with some nanotechnologies, the new comprehension of protein-emulsifier interactions may promote food delivery systems. The research aims to develop an in-depth analysis of interfacial proteins, and provide more innovative and tailored functionalities for the application of the plant protein emulsion.

Indexed as

competition adsorptionmono- and diglyceridespea protein isolatequantitative protein proteomics

Identifiers

PMID38201204
PMCPMC10779286
OpenAlexW4390614951

What OpenQuestion holds

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LicenceCC BY
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.