Atividade antitríptica em semente e produto alimentício de Chia (Salvia Hispanica L.)

Objective: This study aimed to detect anti-tryptic activity in commercial chia seed and flour and to isolate a trypsin inhibitor present in the seed. Methodology: Protein extraction, ammonium sulfate fractionation, affinity chromatography, trypsin inhibition assay, protein quantification and sodium...

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Detalles Bibliográficos
Autores: Morais, Ana Heloneida de Araújo, Souza, Ana Paula Araújo de, Nascimento, Lorena Maria Araújo Marinheiro, Lima, Vanessa Cristina Oliveira de, Carvalho, Fabiana Maria Coimbra de, Santos, Elizeu Antunes dos
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:Brasil
Institución:Universidade Federal do Rio Grande do Norte (UFRN)
Repositorio:Repositório Institucional da UFRN
Idioma:portugués
OAI Identifier:oai:repositorio.ufrn.br:123456789/58129
Acceso en línea:https://repositorio.ufrn.br/handle/123456789/58129
http://dx.doi.org/10.12957/demetra.2017.25636
Access Level:acceso abierto
Palabra clave:Farinha
Sementes
Inibidores de proteases
Tripsina
Flour
Protein
Enzyme inhibitors
Trypsin
Descripción
Sumario:Objective: This study aimed to detect anti-tryptic activity in commercial chia seed and flour and to isolate a trypsin inhibitor present in the seed. Methodology: Protein extraction, ammonium sulfate fractionation, affinity chromatography, trypsin inhibition assay, protein quantification and sodium dodecyl sulfate polyacrylamide gel electrophoresis were performed. Results and discussion: From the retained protein peak in the affinity column, 51% and 64% of anti-tryptic activity for chia flour and seed were respectively found. Large amounts of soluble proteins were not observed in the retained protein peaks of both chia seed and flour, when compared to the crude extract and protein fractions. The trypsin inhibitor in the seed was isolated, with an estimated molecular mass of approximately 14.4 kDa. Conclusions: In view of the unprecedented results regarding the detection of anti-tryptic activity in commercial chia seed and flour, and isolation of the inhibitor in the seed, further research is needed on this new molecule, regarding its bioactive properties and safe consumption