Evidence map›Paper›PMID 29439533›Full record

ArticleMolecules (Basel, Switzerland)2018

Molecular and Functional Properties of Protein Fractions and Isolate from Cashew Nut (Anacardium occidentale L.).

Cheng-Mei Liu, Qian Peng, Jun-Zhen Zhong, Wei Liu, Ye-Jun Zhong, Fang Wang

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
–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

27 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Plant-based foods as meat and fat substitutes.Food science & nutrition · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Consumption of Cashew (Nutrients · 2022
    Article
  17. Article
  18. Review
  19. Correlating the morphology ofFrontiers in plant science · 2022
    Article
  20. 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.

Cheng-Mei LiuState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. liuchengmei@aliyun.com.
Qian PengState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. ncupengqian@163.com.
Jun-Zhen ZhongState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. zhongjunzhen@163.com.
Wei LiuState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. liuwei@ncu.edu.cn.
Ye-Jun ZhongState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. zhongyejun@ncu.edu.cn.
Fang WangState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. ncuskwfang@163.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some molecular and functional properties of albumin (83.6% protein), globulin (95.5% protein), glutelin (81.3% protein) as well as protein isolate (80.7% protein) from cashew nut were investigated. These proteins were subjected to molecular (circular dichroism, gel electrophoresis, scanning electron microscopy) and functional (solubility, emulsification, foaming, water/oil holding capacity) tests. Cashew nut proteins represent an abundant nutrient with well-balanced amino acid composition and could meet the requirements recommended by FAO/WHO. SDS-PAGE pattern indicated cashew nut proteins were mainly composed of a polypeptide with molecular weight (MW) of 53 kDa, which presented two bands with MW of 32 and 21 kDa under reducing conditions. The far-UV CD spectra indicated that cashew proteins were rich in β-sheets. The surface hydrophobicity of the protein isolate was higher than that of the protein fractions. In pH 7.0, the solubility of protein fractions was above 70%, which was higher than protein isolate at any pH. Glutelin had the highest water/oil holding capacity and foaming properties. Protein isolate displayed better emulsifying properties than protein fractions. In summary, cashew nut kernel proteins have potential as valuable nutrition sources and could be used effectively in the food industry.

Indexed as

AlbuminsAnacardiumDietary ProteinsElectrophoresis, Polyacrylamide GelFood AnalysisGlobulinsGlutensHydrogen-Ion ConcentrationMolecular WeightNutsPlant ProteinsProtein Conformation, beta-StrandSolubilityAlbuminsDietary ProteinsGlobulinsGlutensPlant Proteinscashew nutfunctional propertiesphysicochemical characterizationprotein fraction

Identifiers

PMID29439533
PMCPMC6016967

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.