Evidence map›Paper›PMID 33755896›Full record

ArticlePlant foods for human nutrition (Dordrecht, Netherlands)2021

Extraction and Characterization of Proteins from Pachyrhizus ahipa Roots: an Unexploited Protein-Rich Crop.

Cecilia Dini, A V Quiroga, S Z Viña, M A García

Abstract read
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In one paragraph

Article in Plant foods for human nutrition (Dordrecht, Netherlands), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
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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

4 authors.

Cecilia DiniCIDCA (Centro de Investigación y Desarrollo en Criotecnología de Alimentos), Facultad de Ciencias Exactas UNLP - CONICET La Plata - CICPBA, 47 y 116 S/N, 1900, La Plata, Buenos Aires, Argentina. cdini@biol.unlp.edu.ar.ORCID http://orcid.org/0000-0002-2780-6261
A V QuirogaCIDCA (Centro de Investigación y Desarrollo en Criotecnología de Alimentos), Facultad de Ciencias Exactas UNLP - CONICET La Plata - CICPBA, 47 y 116 S/N, 1900, La Plata, Buenos Aires, Argentina.ORCID https://orcid.org/0000-0001-9086-6163
S Z ViñaCIDCA (Centro de Investigación y Desarrollo en Criotecnología de Alimentos), Facultad de Ciencias Exactas UNLP - CONICET La Plata - CICPBA, 47 y 116 S/N, 1900, La Plata, Buenos Aires, Argentina.ORCID https://orcid.org/0000-0002-2948-5609
M A GarcíaCIDCA (Centro de Investigación y Desarrollo en Criotecnología de Alimentos), Facultad de Ciencias Exactas UNLP - CONICET La Plata - CICPBA, 47 y 116 S/N, 1900, La Plata, Buenos Aires, Argentina.ORCID https://orcid.org/0000-0002-4292-7889

Funding

Consejo Nacional de Investigaciones Científicas y Técnicas PIP 0555 2013-2015Fondo para la Investigación Científica y Tecnológica PICT 2015-0921Fondo para la Investigación Científica y Tecnológica PICT 2015-3249
6 · The paper itself

Abstract

Pachyrhizus ahipa is an unexploited crop known to be rich in proteins compared to other edible roots and tubers. These proteins are not prolamins, thus ahipa represents an interesting new source of ingredients for gluten-free foods. In this work, ahipa proteins (AP) were extracted and partially characterized in pursuit of their use as food ingredients. The effect of ultrasound treatment on protein extraction efficiency was evaluated. AP were characterized by their size, amino acid composition, surface hydrophobicity, intrinsic fluorescence, FTIR spectra, solubility, and thermal and emulsifying properties. AP were efficiently removed from the vegetal tissue using PBS or water, regardless of the use of ultrasound, but not easily recovered by precipitation. This protein fraction was composed of small proteins, with sizes ranging from 9 to 30 kDa, and highly polar. AP resulted particularly rich in aspartic acid (59% of the total amino acid content), for which they can be classified as Asp-rich proteins. Their elevated content of acidic groups was evidenced in the ATR-FTIR spectrum. The amide I band deconvolution as well as the low surface hydrophobicity and denaturation enthalpy indicated that these proteins are mainly unordered structures. The emulsifying properties of AP were enhanced when the concentration was increased from 0.1 to 1% (w/v) but resulted lower than those of soy protein. The high polarity, small size, and low isoelectric point make AP particularly suitable for acidic food matrices.

Indexed as

PachyrhizusHydrophobic and Hydrophilic InteractionsPlant RootsSolubilityWaterWaterAcidic proteinsAhipa rootsAspartic acidFood proteinsGluten-free ingredientsTuberous roots

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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.