Evidence map›Paper›PMID 34262733›Full record

ReviewFood science & nutrition2021

Pea protein isolate characteristics modulate functional properties of pea protein-cranberry polyphenol particles.

Renee Cilliers Strauch, Mary Ann Lila

Open access · hybridAbstract readReview
In one paragraph

Review in Food science & nutrition, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

13 citing papers in PubMed, 49 citations in OpenAlex.

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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 at 1 institution in 1 country.

Renee Cilliers StrauchPlants for Human Health Institute North Carolina State University Kannapolis NC USA.ORCID https://orcid.org/0000-0002-9376-6683
Mary Ann LilaPlants for Human Health Institute North Carolina State University Kannapolis NC USA.ORCID https://orcid.org/0000-0002-4928-3836
North Carolina State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant polyphenols have a natural binding affinity for proteins, and their interaction can be exploited to form diverse aggregate particles. Protein-polyphenol particles utilized as food ingredients allow consumers to incorporate more health-benefiting plant bioactives into their diets. The functional properties of the protein-polyphenol particles can be influenced by many factors, including complexation conditions and starting material properties. Here, cranberry polyphenols extracted from pomace were complexed with nine pea protein isolate starting materials with different physical (particle size and protein content) and chemical (hydrolyzed and oxidized) properties to investigate the impact of protein characteristics on particle functionality. Chemical differences between proteins affected polyphenol binding; oxidized protein isolate (specifically, VegOtein N) bound 12%-27% more polyphenols than other isolates. Polyphenol binding to proteins decreased digestion rates in vitro, averaging 25% slower gastric (pepsin) digestion and a 35% slower intestinal (pancreatin) digestion. Physical differences in protein starting materials affected digestibility; isolate with the largest particle size (specifically, Nutralys F85G) produced particles with the lowest digestion rate. Solubility was impacted by both the process of forming particles and by polyphenol binding; control particles were 56% less soluble, and protein-polyphenol particles up to 75% less soluble, than unmodified proteins. The solubility of unmodified protein isolate starting materials varied widely according to the manufacturing process, but, after complexation, protein-polyphenol particles produced from all protein sources exhibited a similar depressed level of solubility. The desired functional properties of the protein-polyphenol particle food ingredients will be considerably influenced by the properties of the protein isolate starting material.

Indexed as

by‐productscranberry polyphenolsdigestionpea protein isolatesolubility

Identifiers

PMID34262733
PMCPMC8269610
OpenAlexW3164037068

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.