Evidence map›Paper›PMID 35804636›Full record

ArticleFoods (Basel, Switzerland)2022

Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions.

Xiaopeng Qin, Linbo Li, Xiao Yu, Qianchun Deng, Qisen Xiang, Yingying Zhu

Abstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2022. 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
–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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Proteomic Profile of Flaxseed (Foods (Basel, Switzerland) · 2024
    Article
  4. Review
  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

6 authors.

Xiaopeng QinCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China.
Linbo LiCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China.
Xiao YuCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China.
Qianchun DengOil Crops Research Institute, Chinese Academy of Agricultural Sciences, Wuhan 430062, China.
Qisen XiangCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China.
Yingying ZhuCollege of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China.

Funding

National Natural Science Foundation of China 32072267
6 · The paper itself

Abstract

This study aimed to comparatively elucidate the composition structure and techno-functionality of flaxseed protein isolate (FPI), globulin (FG), and albumin (FA) fractions. The results showed that FA possessed smaller particle dimensions and superior protein solubility compared to that of FG (p < 0.05) due to the lower molecular weight and hydrophobicity. FA and FG manifested lamellar structure and nearly spherical morphology, respectively, whereas FPI exhibited small lamellar strip structure packed by the blurring spheres. The Far-UV CD, FTIR spectrum, and intrinsic fluorescence confirmed more flexible conformation of FA than that of FG, followed by FPI. The preferential retention of free phenolic acids was observed for FA, leading to excellent antioxidant activities compared with that of FG in FPI (p < 0.05). FA contributed to the foaming properties of FPI, relying on the earlier interfacial adsorption and higher viscoelastic properties. FA displayed favorable emulsifying capacity but inferior stability due to the limited interfacial adsorption and deformation, as well as loose/porous interface. By comparison, an interlayer anchoring but no direct interface coating was observed for lipid droplets constructed by FG, thereby leading to preferable emulsion stability. However, FPI produced lipid droplets with dense interface owing to the effective migration of FA and FG from bulk phase, concomitant with the easy flocculation and coalescence. Thus, the techno-functionality of flaxseed protein could be tailed by modulating the retention of albumin fraction and specific phenolic acids.

Indexed as

component structureflaxseed protein fractionsinterfacial behaviorphenolic acidstechno-functionality

Identifiers

PMID35804636
PMCPMC9265867

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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.