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Cowpea protein concentrate: A detailed analysis of composition, structure, and technological properties

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Autor(es):
de Oliveira, Maria Mariana Garcia ; Fessori, Ana Gabriela Baroni Wicher ; Huamani-Melendez, Victor Justiniano ; Mauro, Maria Aparecida
Número total de Autores: 4
Tipo de documento: Artigo Científico
Fonte: Food Research International; v. 213, p. 13-pg., 2025-08-01.
Resumo

Cowpea, an underutilized and nutritive alternative plant protein source, offers a potential solution to climate change and population growth, but still requires extensive research. This study aimed to comprehensively assess the properties and techno-functional responses of cowpea protein concentrate (CPC) under various pH conditions in an integrated way, with a particular emphasis on the CPC's application potential. CPC was extracted and analyzed in both powdered and solution forms, the former under different pH conditions. CPC exhibited a diverse size distribution, with intense bands around 50 kDa, corresponding to globulins, especially vicilins. Trypsin inhibitor (TI) in CPC was reduced by approximate to 70 % due to leaching and disulfide bond disruption. The protein profile of cowpeas demonstrated an adequate proportion of essential amino acids, with leucine standing out (6.07 g AA & sdot;100 g(-1) CPC). CPC reveals an amorphous structure, with its secondary structure primarily composed of beta-sheet, characterizing the 7S protein fraction. The elevated denaturation temperature (131.86 degrees C) of CPC is indicative of its high thermostability. CPC exhibited a greater affinity for oil (1.72 g & sdot;g(-1) CPC) than water (1.37 g & sdot;g(-1) CPC), conferring advantageous properties on oil-rich food formulations. pH influenced CPC's techno-functional properties, particularly solubility, emulsifying capacity, and foaming ability. Solubility was low at pH 3 and 5, whereas alkaline conditions enhanced stability. CPC demonstrated strong foaming capacity (>60 %) and stability (approximate to 100 %) across all pH range, and high emulsifying capacity (>1000 g oil/g protein). The reduction of TIs, along with their thermal stability, emulsifying and foaming capabilities, underscore CPC's potential for a wide range of food applications. (AU)

Processo FAPESP: 20/05254-4 - Estruturação de materiais alimentícios de origem vegetal na forma de emulsões, biofilmes, espumas e organogéis
Beneficiário:Maria Aparecida Mauro
Modalidade de apoio: Auxílio à Pesquisa - Regular
Processo FAPESP: 21/08321-7 - Extração e caracterização de proteína de feijão-caupi e aplicações em emulsões, filmes e microcápsulas
Beneficiário:Víctor Justiniano Huamaní Meléndez
Modalidade de apoio: Bolsas no Brasil - Programa Capacitação - Treinamento Técnico