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Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions

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Abstract

Pigeon pea protein isolates (PPI) are an option to obtain a high yield of good quality proteins and represent a great potential for the food industry. In this work, physicochemical and structural properties of albumin (ALB), globulin (GLB), and PPI obtained at different pHs (8, 9, 10, and 11) were studied to deepen the knowledge of these proteins for future application. GLB presented protein aggregates and polypeptides characteristics of 7S vicilin subunits while ALB presented polypeptides with low molecular masses. GLB showed a more compact and less flexible structure than ALB fraction due to the distinct conformational characteristics found in DSC, fluorescence spectroscopy, Ho. These structural characteristics conferred GLB greater conformational stability (∆GH2O) than ALB fraction. The latter presented a higher proportion of β-strand in aggregated structures. PPI11 showed the highest protein recovery, but the least So with more presence of protein aggregates with the least proportion of β-strands in aggregated structures. A higher percentage of protein unfolding and exposure of hydrophobic residues to solvent was observed as the extraction pH of the isolates increased. Enthalpy change of transition decreased, and the maximum emission wavelength shifted to red in fluorescence spectroscopy. However, PPI11 showed only a slight increase in Ho (10%) with respect to PPI8. The variation in pH for protein extraction constitutes a simple, rapid, and low-cost method to obtain PPI with physicochemical and structural properties that will determine its functional properties and their use as food ingredients.

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Abbreviations

ALB:

albumin fraction

GLB:

globulin fraction

ΔH:

enthalpy change of transition

FI:

fluorescence intensity

∆GH2O :

free energy of denaturation

λmax :

maximum emission wavelength

2-ME:

2-mercaptoethanol

MW:

molecular weight

PI:

protein isolates

PP:

pigeon pea

PPI:

pigeon pea protein isolates

SEC:

size exclusion chromatography

So:

protein solubility

Td:

denaturation temperature

Trp:

Tryptophan

V0 :

void volume of the column

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Funding

The authors acknowledge the financial support from the Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT) and the Universidad Nacional del Nordeste (UNNE) and CONICET, Argentina. M. V. Avanza and A. V. Quiroga are research members of the Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET).

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Authors and Affiliations

  1. Facultad de Ciencias Exactas y Naturales y Agrimensura, Universidad Nacional del Nordeste (UNNE) and Instituto de Química Básica y Aplicada del Nordeste Argentino (IQUIBANEA) UNNE-CONICET, Avenida Libertad 5470, 3400, Corrientes, República Argentina

    Eliana Isabel Fernández Sosa, María Guadalupe Chaves & María Victoria Avanza

  2. Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA) UNLP-CONICET, 47 y 116, 1900, La Plata, República Argentina

    Alejandra Viviana Quiroga

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  1. Eliana Isabel Fernández Sosa
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  2. María Guadalupe Chaves
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  3. Alejandra Viviana Quiroga
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  4. María Victoria Avanza
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Correspondence to Eliana Isabel Fernández Sosa.

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Fernández Sosa, E.I., Chaves, M.G., Quiroga, A.V. et al. Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions. Plant Foods Hum Nutr 76, 37–45 (2021). https://doi.org/10.1007/s11130-020-00871-7

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