Evidence map›Paper›PMID 32268602›Full record

ReviewInternational journal of molecular sciences2020

Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute.

Vilia Darma Paramita, Naksit Panyoyai, Stefan Kasapis

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

5 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Peas (Molecules (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Article
  5. 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

3 authors at 3 institutions in 2 countries.

Vilia Darma ParamitaDepartment of Chemical Engineering, State Polytechnic of Ujung Pandang, Tamalanrea, Makassar 90245, Indonesia.
Naksit PanyoyaiDepartment of Agroindustry, Rajabhat Chiang Mai University, Chiang Mai 50330, Thailand.
Stefan KasapisSchool of Science, RMIT University, Bundoora West Campus, Plenty Road, Melbourne, Vic 3083, Australia.
Chiang Mai Rajabhat University · THPoliteknik Negeri Ujung PandangRMIT University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the food industry, proteins are regarded as multifunctional systems whose bioactive hetero-polymeric properties are affected by physicochemical interactions with the surrounding components in formulations. Due to their nutritional value, plant proteins are increasingly considered by the new product developer to provide three-dimensional assemblies of required structure, texture, solubility and interfacial/bulk stability with physical, chemical or enzymatic treatment. This molecular flexibility allows them to form systems for the preservation of fresh food, retention of good nutrition and interaction with a range of microconstituents. While, animal- and milk-based proteins have been widely discussed in the literature, the role of plant proteins in the development of functional foods with enhanced nutritional profile and targeted physiological effects can be further explored. This review aims to look into the molecular functionality of plant proteins in relation to the transport of bioactive ingredients and interaction with other ligands and proteins. In doing so, it will consider preparations from low- to high-solids and the effect of structural transformation via gelation, phase separation and vitrification on protein functionality as a delivery vehicle or heterologous complex. Applications for the design of novel functional foods and nutraceuticals will also be discussed.

Indexed as

AlgorithmsBinding SitesChemical PhenomenaFood TechnologyFunctional FoodKineticsLigandsModels, MolecularModels, TheoreticalMolecular ConformationNutritive ValuePlant ProteinsProtein BindingStructure-Activity RelationshipTemperatureThermodynamicsLigandsPlant Proteinsdiffusionlow- to high-solid systemsplant proteinsprotein-ligand interactions

Identifiers

PMID32268602
PMCPMC7178117
OpenAlexW3014655030

What OpenQuestion holds

Textmetadata
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.