Large-Scale Chromatography for the Isolation of 7S Globulin Enriched Fraction from Pigeon Pea Seeds

Pigeon pea (<i>Cajanus cajan</i>) contains around 60% globulin proteins, of which 7S globulin is the most abundant fraction. In this work, a purification protocol for pigeon pea 7S globulin was developed using large-scale chromatography. The process was designed on an analytical scale through desalting of the crude protein extract followed by anion exchange chromatography and size exclusion chromatography. Then, the process was scaled up to a large scale. The purified fraction presented a protein content of 89 g/100 g powder and yield close to 23%. The isolated 7S globulin showed two main subunits of 64 and 49 kDa, identified as the α- and β-chains of β-conglycinin by proteomic analysis. The developed protocol was shown to be suitable for purifying pigeon pea 7S globulin on a large scale, and it is relevant for isolating this fraction from other pulse seeds in sufficient quantities for their characterization and evaluation of functional properties.

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Publication Details

Journal
Journal of Agricultural and Food Chemistry
Published
2025-04-24
DOI
https://doi.org/10.1021/acs.jafc.5c01681
Citations
2
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
2.32

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article

Large-Scale Chromatography for the Isolation of 7S Globulin Enriched Fraction from Pigeon Pea Seeds

Hélène Rogniaux, Joëlle Davy, Hanitra Rabesona, Hamza Mameri et al.
2 citations
Journal of Agricultural and Food Chemistry
Proteins in Food Systems
2.32
article

Large-Scale Chromatography for the Isolation of 7S Globulin Enriched Fraction from Pigeon Pea Seeds

Hélène Rogniaux, Joëlle Davy, Hanitra Rabesona, Hamza Mameri, Sophie Le Gall, Sophie Laurent, Véronique Solé-Jamault, Claire Berton‐Carabin, Adilson Roberto Locali-Pereira, Adeline Boire, Valérie Beaumal, Vânia Regina Nicoletti, Mehdi Cherkaoui
article en
2 citations

Abstract

Pigeon pea (<i>Cajanus cajan</i>) contains around 60% globulin proteins, of which 7S globulin is the most abundant fraction. In this work, a purification protocol for pigeon pea 7S globulin was developed using large-scale chromatography. The process was designed on an analytical scale through desalting of the crude protein extract followed by anion exchange chromatography and size exclusion chromatography. Then, the process was scaled up to a large scale. The purified fraction presented a protein content of 89 g/100 g powder and yield close to 23%. The isolated 7S globulin showed two main subunits of 64 and 49 kDa, identified as the α- and β-chains of β-conglycinin by proteomic analysis. The developed protocol was shown to be suitable for purifying pigeon pea 7S globulin on a large scale, and it is relevant for isolating this fraction from other pulse seeds in sufficient quantities for their characterization and evaluation of functional properties.

Journal of Agricultural and Food ChemistryVol. 73(18)
Université de Montpellier (FR), Ingénierie des Agropolymères et Technologies Emergentes (FR), Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR), Universidade Estadual Paulista (Unesp) (BR), Wageningen University & Research (NL)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Ministère de l'Europe et des Affaires Étrangères, Division of Graduate Education
Zero hunger
Openalex Percentile: Top 13%
Proteins in Food Systems
2.32
DOIOpen Access PDFOpenAlex
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