Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH英文电子书.pdf

Food Research International 69 (2015) 216–223 Contents lists available at ScienceDirect Food Research International journal homepage: www. /locate/food res Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH Raúl E. Cian a,b,⁎, Javier Vioque c, Silvina R. Drago a,b a Facultad de Ingeniería Química, Instituto de Tecnología de Alimentos, Universidad Nacional del Litoral, 1° de Mayo 3250, Santa Fe 3000, República Argentina b Consejo Nacional de Investigaciones Científi cas y Técnicas (CONICET), Av. Rivadavia 1917, Ciudad de Buenos Aires C1033AAJ, República Argentina c Instituto de la Grasa, CSIC, Avda. Padre García Tejero 4, Sevilla 41012, Spain a r t i c l e i n f o a b s t r a c t Article history: The aims of this study were to assess bioactive properties (ACE inhibition and antioxidant capacity) from wheat Received 23 September 2014 gluten hydrolysate peptides fractionated by pH (4.0, 6.0 and 9.0), to determine peptide action mechanism, and to Accepted 23 December 2014 relate it to the secondary structure and functional groups of peptides. Gluten hydrolysate extracts (GHE) were Available online 2 January 2015 enriched in peptides with medium hydrophobicity and molecular weight (≈60% MH and 5.5 kDa, respectively). Gluten peptides inhibited ACE I by uncompetitive mechanism and a direct relationship between α-helix Keywords: