Evidence map›Paper›PMID 36082141›Full record

ArticleCurrent research in food science2022

Wheat gluten proteins phosphorylated with sodium tripolyphosphate: Changes in structure to improve functional properties for expanding applications.

Fei Hu, Peng-Ren Zou, Fan Zhang, Kiran Thakur, Mohammad Rizwan Khan, Rosa Busquets, Jian-Guo Zhang, Zhao-Jun Wei

Open access · goldAbstract read
In one paragraph

Article in Current research in food science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

8 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. 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

8 authors at 3 institutions in 3 countries.

Fei HuSchool of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
Peng-Ren ZouSchool of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
Fan ZhangSchool of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
Kiran ThakurSchool of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
Mohammad Rizwan KhanDepartment of Chemistry, College of Science, King Saud University, Riyadh, 11451, Saudi Arabia.
Rosa BusquetsSchool of Life Sciences, Pharmacy and Chemistry, Kingston University London, Kingston Upon Thames, KT1 2EE, Surrey, England, UK.
Jian-Guo ZhangSchool of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
Zhao-Jun WeiSchool of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
Hefei University of Technology · CNKing Saud University · SAKingston University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poor solubility of wheat gluten proteins (WG) has negative impact on functional attributes such as gelation and emulsification, which limits it use in the food industry. In this study, WG underwent different degrees of phosphorylation using sodium tripolyphosphate (STP). Phosphoric acid groups were successfully incorporated in the WG via covalent bonding (C-N-P and C-O-P) involving hydroxyl and primary amino groups from WG. The introduction of phosphoric acid groups increased the negative charge of phosphorylation-WG, which caused the enhancement of electrostatic repulsion between proteins and reduced the droplet size in emulsions, thereby allowing proteins to be more efficiently dispersed in the solution system. The change of structure induced with phosphorylation improved hydration of protein, making the WG with higher solubility, thereby resulting in the improvement of its emulsification, foaming, thermal stability, and rheological properties. Therefore, WG can be modified by phosphorylation which caused an overall improvement of functional properties, thus facilitating the expansion of WG applications.

Indexed as

Functional propertiesPhosphorylationSolubilityWheat gluten proteinsX-ray photoelectron spectroscopy

Identifiers

PMID36082141
PMCPMC9445281
OpenAlexW4293378894

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.