IDENTIFICATION OF PEPTIDES WITH BIOACTIVE POTENTIAL IN WITBIER STYLE CRAFT BEER

Beer is the result of the fermentation process of the brewer's wort, which has barley or wheat malts, unmalted cereals, water, and hops in its composition. In the brewing, the wort is subjected to different time and temperature gradients that allow the action of the malt enzymes for the hydrolysis of sugars and proteins. These chemical and biochemical reactions influence the nutritional composition of the beer. Attributes that establish the quality of beers such as flavor, foam firmness and colloidal stability are related to their composition of proteins and peptides. Despite the large worldwide consumption of beer, knowledge about its protein content is still quite limited. Most of the proteins identified in beer come from barley malts, unmalted cereals such as corn, oats and wheat, and fermentation yeasts. Furthermore, little information is found on the composition of beer peptides. Peptides with 2 to 20 amino acid residues have already been described as bioactive and with positive physiological effects in vivo. Antioxidant activity and antihypertensive effects are some of the roles that bioactive peptides can play in the body. They originate from endogenous sources or are obtained from the diet. Thus, the objective of this work was to investigate the presence of di- and tri-peptides with bioactive potential in a sample of Witbier style beer containing barley malt, wheat, and Sicilian lemon in its composition. Analyses were performed using LC-MS/MS through the 46 Da neutral loss and collision-induced dissociation methods, followed by research on the biological activity of these molecules in the BIOPEP database. Six dipeptides with bioactive potential were identified, three of which exhibit activity in the inhibition of angiotensin-converting enzyme I (ACE I), causing blood vasoconstriction and resultant increase in blood pressure, as well as activity in the prevention of diabetes mellitus through the inhibition of dipeptidyl peptidase IV (DPP-IV). The other three dipeptides exhibit only activity in the inhibition of DPP-IV, which is responsible for the hydrolysis of glucagon, a hormone regulating blood glucose levels. These results contribute to the development of new studies to evaluate the peptide composition of beers and their potential health benefits.