Characterization of the peptide profile in Spanish Teruel, Italian Parma and Belgian dry-cured hams and its potential bioactivity

Dry-cured hams are appreciated products in many European countries. One of the most important processes taking place during ham processing and responsible for its unique taste and flavour is the proteolysis of muscle proteins. Muscle peptidases play an important role in breaking down muscle proteins and generating small peptides and free amino adds. It is known that changes in genetics and processing conditions can result in differences in the action of endopeptidases and exopeptidases. In this study, the peptides generated in Spanish Teruel, Italian Parma and Belgian dry-cured hams have been identified and quantified using a label-free methodology to assess main differences in proteolysis between the 3 types of hams. The identification of the peptides resulted in differential peptide sequences according to the type of ham. On the other hand, an aqueous peptide extract fractionated by size-exclusion chromatography was assayed for Angiotensin-Converting Enzyme (ACE) inhibitory and antioxidant activity. Peptide fractions of Teruel ham exhibited 93% ACE inhibition while those from Parma and Belgian hams had ACE inhibitory activity of 70% and 76%, respectively. The investigated peptide fractions exhibited similar values of DPPH scavenging activity whereas an important Fe2+ reducing power was also detected in the same fractions, suggesting the important presence of peptides with antioxidant activity in the three studied types of dry-cured hams. (C) 2016 Elsevier Ltd. All rights reserved.