As bovine whey is a continuous problem in worldwide pollution, emerging technologies have been proposed to take advantage of its organic composition and thus implement sustainable biorefining. A strategy for mitigating whey contamination and valorizing it is the development of protein-based beverages or healthier food products. Therefore, this work aimed to obtain a whey hydrolysate using pancreatin, which can be incorporated as a functional ingredient in antihypertensive formulations. Whey dispersions at 10 % (w/v) were prepared in Tris-HCl buffer (0.02 M, pH=8) and thermal treated at 90 °C for 10 min. Then, pancreatin hydrolysis was carried out for 7 h by enzyme addition in a mass ratio of 100:4 (soluble protein: enzyme) and sampling each hour. Free amino groups production was followed by the trinitrobenzene sulfonic acid method, and a Tukey’s contrast was performed to determine significant differences between sampling times and only test its ACE inhibitory capacity by hippuric acid determination in those that show significant differences. Afterward, a functional beverage was prepared according to the formulation proposed for a local ice cream bases factory, which contained water (77%), fructose (13%), hydrolyzed whey protein (7.7%), butyric fat (1%), flavoring (0.32%), stabilizing salts (0.17%), and emulsifier (0.1%), and its antihypertensive activity was measured by in vitro ACE inhibition. Pancreatin hydrolysis of bovine whey produced free amino groups with statistically significant differences at times 0, 4, and 7 h (p<0.05), having a concentration of 748.04±67.64, 727.39±7.69, and 1206.74±138.35 mg/L, respectively. The ACE inhibition for those sampling times was 32.41±0.63 (0 h), 16.67±1.57 (4 h), and 29.63±1.10 % (7 h). Due to Tukey’s contrast showed no differences between the sampling times 0 and 7 h, both were incorporated into the antihypertensive beverage formulation, and their ACE inhibition capacity was tested in the final product, founding an inhibition percentage of 74.84±1.39% and 78.76±1.39% with the 0 and 7 h hydrolysates, respectively. The increasing inhibition was associated with the pH buffering at 6.69, originating from the stabilizing salts and used for pancreatin hydrolysates generation incorporated in the beverages to make compatible manufacturer formulations with the previously designed enzymatic process. Nonetheless, the antihypertensive activity showed the same trend found once, with no significant differences (p<0.05) among the hydrolysates tested (0 and 7 h). Finally, despite the ACE inhibition power being the same for the times 0 and 7 h in the kinetic systems as in the final beverage formulation, a preliminary sensory analysis showed that the product based on the 7 h hydrolysate could have better acceptability because it exhibited less salty taste.