Evaluation of surfactant activity and emulsifying of Pea protein isolate (Pisum sativum L.) obtained by the spray dryer

ABSTRACT This study evaluates the biosurfactant activity and emulsification ability of pea proteins isolated (Pisum sativum L.). The results showed that aqueous solutions containing the pea proteins isolated (PPI) reduce the water surface tension to 47mN/m, approximately. The use of spray dryer does...

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Detalles Bibliográficos
Autores: Mendes,Anderson Nogueira, Kelber,Natasha, Filgueiras,Lívia Alves, Costa,Camila Sousa Campos da, Porto,Cristiana Pedrosa Melo, Pierucci,Anna Paola Trindade Rocha, Nele,Márcio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:Brasil
Institución:Matéria (Rio de Janeiro. Online)
Repositorio:Matéria (Rio de Janeiro. Online)
Idioma:inglés
OAI Identifier:oai:scielo:S1517-70762018000400404
Acceso en línea:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-70762018000400404
Access Level:acceso abierto
Palabra clave:biosurfactant
vegetable protein
globulin
spray dryer
pea protein isolated
Descripción
Sumario:ABSTRACT This study evaluates the biosurfactant activity and emulsification ability of pea proteins isolated (Pisum sativum L.). The results showed that aqueous solutions containing the pea proteins isolated (PPI) reduce the water surface tension to 47mN/m, approximately. The use of spray dryer does not change the surfactant activity of the PPI because surface tension and CMC will not change. The PPI is thermally stable and can be used in processes that require temperatures between 4°C and 80°C, as industrial processes such as baking, ice cream and other formulation. The protein isolate and pea assessed emulsions with toluene and n-heptane were stable. Emulsions castor and linseed oil were not stable under the conditions reported in this paper. Therefore, despite the pea protein isolate is a surfactant it cannot be used in any industrial process. Both the food industry and in the biotechnology industry should evaluate the conditions for application of protein isolates from pea.