Julio Girón-Calle

TL;DR: In this article, the authors showed that legumin with alcalase yielded a hydrolysate that inhibited the angiotensin I-converting enzyme with an IC 50 of 0.18 mg/ml.

TL;DR: Results show that sunflower seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with pepsin and pancreatin.

TL;DR: It was observed that the number of lysine residues that took part in the immobilization process was a consequence of the type of support and reaction time of the experimental conditions, and that the increasing of the thermal stability of the derivatives was correlated with a increasing number ofLysines residues involved in a multipoint covalent attachment.

TL;DR: Fractions coming from the isolate and phaseolin had similar activities except for iron chelation, suggesting that phaseolin is the major contributor to the antioxidant and copper chelating activities of the hydrolysed protein isolate.

TL;DR: In this paper, the authors used protein hydrolysates for the purification of ACE-inhibitory peptides using protease alcalase and Biogel P2 gel filtration chromatography and HPLC C 18 reverse phase chromatography.