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

Abstract

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