Obtaining of peptides with in vitro antioxidant and angiotensin I converting enzyme inhibitory activities from canihua protein (Chenopodium pallidicaule Check for Aellen)

Hydrolysates and peptides from a canihua protein concentrate with antioxidant and angiotensine-I converting enzyme (ACE) inhibitory activities were evaluated in vitro. Hydrolysates were obtained via enzymatic hydrolysis using: Alcalase, Neutrase and Flavourzyme, in reaction in one and two sequential stages. The protein hydrolysate obtained in two sequential stages (Neutrase-Alcalase for 180 min at 50 degrees C), presented the highest antioxidant activity and ACE inhibition (2.12 mu mol TE/mg and 69.8%, respectively) and a low IC50 value (0.12 mg/mL). This hydrolysate was further purified through ultrafiltration with membranes of cut off values of 10 and 3 kDa, followed by size exclusion chromatography and a total of three fractions were obtained (F-I, F-II and F-III, respectively). LC-MS/MS analysis revealed peptides composed of 3-11 aminoacids in F-II and F-III which were identified via cross species identification within the polypeptidic chain of protein 11S seed globulin of Chenopodiwn quinoa. F-Ill outstood in the evaluated bioactive properties (3.18 mol TE/mg, 78.4% and 55 h mu g/mL). Up to our knowledge, this is the first study focused on obtaining of protein hydrolysates and peptides with bioactive properties from canihua. These results could be used to obtain products from canihua with added value as potential functional ingredients.