Evaluation of oxidative hemolytic inhibition capacity and antimicrobial activity of peptide fractions from egg, milk and soy protein hydrolysis using Bromelia pinguin and Bromelia karatas derived proteases

Protein hydrolysates are a source of bioactive peptides (BP). They can exert an important role in human health due to their different biological activities. The use of plant proteases is a potential alternative to produce BP. The aim of this work was to evaluate the oxidative hemolytic inhibition ca...

Descripción completa

Detalles Bibliográficos
Autores: Aguilera-Aguirre, Selene, Meza-Espinoza, Libier, Hernández-Mendoza, Adrián, Vallejo-Córdoba, Belinda, González-Córdova, Aarón F., Montalvo-González, Efigenia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:México
Institución:UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO
Repositorio:TIP Revista especializada en ciencias químico-biológicas
Idioma:español
OAI Identifier:oai:ojs.ojs.escire.net:article/142
Acceso en línea:http://tip.zaragoza.unam.mx/index.php/tip/article/view/142
Access Level:acceso abierto
Palabra clave:oxidative hemolytic inhibition; antimicrobial activity; hydrolysates; peptides
inhibición hemolítica oxidativa; actividad antimicrobiana; hidrolizada; péptidos bioactivos
Descripción
Sumario:Protein hydrolysates are a source of bioactive peptides (BP). They can exert an important role in human health due to their different biological activities. The use of plant proteases is a potential alternative to produce BP. The aim of this work was to evaluate the oxidative hemolytic inhibition capacity (OHI) and antimicrobial activity of hydrolysates and peptide fractions from egg, milk and soy protein hydrolysis with proteases extracted from Bromelia pinguin and Bromelia karatas fruits. In general, all hydrolysates and peptide fractions presented a high OHI, being the peptide fraction of ≤1 kDa from ovalbumin protein hydrolysis with B. karatas proteases that had the greater OHI (98.19%). In contrast, hydrolysates did not register antimicrobial activity, while peptide fractions (≤5, ≤10 y ≤30 kDa), from milk hydrolysis with B. pinguin proteases showed the highest antimicrobial activity against Listeria innocua (22.26-23.79% of inhibition). The results highlight the potential of B. pinguin and B. karatas proteases to hidrolize proteins from different foods, as well as to produce hydrolysates and BP, with high oxidative hemolytic inhibition capacity.