Bioactive peptides derived from whey proteins with angiotensin-converting enzyme inhibitory activity

CECILIA V. CIMINO; CONSTANZA LIGGIERI; BRUNO MARIELA A.; SANDRA E. VAIRO CAVALLI

CABA

Congreso; XLIX Reunión Anual de la SAIB; 2013

SAIB

Food proteins encrypt bioactive peptides that can be released during gastrointestinal digestion or food processing by enzymatic proteolysis. Flowers of Carduae tribe, family Asteraceae, contain aspartic proteinases. The aims of the present work were to isolate proteolytic enzymes from flowers of Arctium minus (Hill) Bernh. (Asteraceae), to obtain protein hydrolyzates from bovine whey with angiotensin-converting enzyme (ACE) inhibitory activity employing the peptidases present in enzyme extracts (EE), and to isolate bioactive peptides responsible for the ACE inhibitory activity. Crude enzyme extracts were prepared by pestle pounding of A. minus flowers at pH 7.0. Pigments and other phenolic compounds were eliminated by size-exclusion chromatography. EE were obtained in the void volume. Whey bovine hydrolyzates were performed with EE and analyzed by SDS-PAGE and MALDI-TOF/MS. Hydrolyzed whey was ultrafiltered, and low molecular fraction (peptide mass ≤ 3000 Da) showed ACE inhibitory activity. Peptides obtained by hydrolysis were analyzed by RP-HPLC (ÄKTA Purifier). From twelve peaks resulting from chromatograms, 22.4% of total ACE inhibitory activity was recovered in the peak with retention time 27.26 min. Hydrolyzates and isolated peptides with ACE inhibitory activity could be potentially used in food industry for formulation of nutraceutical products.