Your browser doesn't support javascript.
loading
Pea protein isolate-soluble soybean polysaccharides electrostatic assembly: effect of pH, biopolymer mass ratio and heat treatment.
Igartúa, Daniela Edith; Balcone, Agustina; Platania, Fedra Agustina; Cabezas, Dario Marcelino; Palazolo, Gonzalo Gastón.
Afiliação
  • Igartúa DE; Laboratorio de Investigación en Funcionalidad y Tecnología de Alimentos (LIFTA), Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Buenos Aires, Argentina.
  • Balcone A; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Ciudad Autónoma de Buenos Aires, Argentina.
  • Platania FA; Laboratorio de Investigación en Funcionalidad y Tecnología de Alimentos (LIFTA), Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Buenos Aires, Argentina.
  • Cabezas DM; Laboratorio de Investigación en Funcionalidad y Tecnología de Alimentos (LIFTA), Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Buenos Aires, Argentina.
  • Palazolo GG; Laboratorio de Investigación en Funcionalidad y Tecnología de Alimentos (LIFTA), Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Buenos Aires, Argentina.
J Sci Food Agric ; 104(12): 7291-7300, 2024 Sep.
Article em En | MEDLINE | ID: mdl-38647043
ABSTRACT

BACKGROUND:

In past years, thousands of protein-polysaccharide complexes have been investigated to modify protein characteristics and functionality in food systems. However, the interaction between pea protein isolate (PPI) and soluble soybean polysaccharide (SSPS) has not been thoroughly characterized yet.

RESULTS:

In the present study, the phase behavior of PPI and SSPS mixtures was analyzed as a function of PPISSPS mixing ratio (11 to 10.10) and pH (7.0 to 2.0), showing that these biopolymers could be electrostatically assembled at 11 to 10.25 mixing ratios and 4.0 to 3.0 pH values. Then, the characteristics of the PPI-SSPS complexes were studied before and after heating (90 °C and 30 min) by ζ-potential, surface hydrophobicity, protein solubility, particle size distribution and physical stability for 56 days. By lowering the pH and PPISSPS mixing ratio, the complexes showed increased solubility, changed 𝜁-potential and higher physical stability. By heating, the complexes presented increased hydrophobicity and physical stability.

CONCLUSION:

Overall, PPI-SSPS complexes increased the protein solubility, reduced the particle size, and changed both the ζ-potential and the surface hydrophobicity with respect to PPI control, allowing stabilization of the colloidal system and broadening the possible applications of these high-quality proteins in acidic food systems. © 2024 Society of Chemical Industry.
Assuntos
Palavras-chave
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Solubilidade / Glycine max / Pisum sativum / Eletricidade Estática / Interações Hidrofóbicas e Hidrofílicas / Proteínas de Ervilha / Temperatura Alta Idioma: En Revista: J Sci Food Agric Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Solubilidade / Glycine max / Pisum sativum / Eletricidade Estática / Interações Hidrofóbicas e Hidrofílicas / Proteínas de Ervilha / Temperatura Alta Idioma: En Revista: J Sci Food Agric Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido