Manufacture of Whey Protein Hydrolysates Using Plant Enzymes: Effect of Processing Conditions and Simulated Gastrointestinal Digestion on Angiotensin-I-Converting Enzyme (ACE) Inhibitory Activity.

Hydrolysis of proteins leads to the release of bioactive peptides with positive impact on human health. Peptides exhibiting antihypertensive properties (i.e., inhibition of angiotensin-I-converting enzyme) are commonly found in whey protein hydrolysates made with enzymes of animal, plant or microbial origin. However, bioactive properties can be influenced by processing conditions and gastrointestinal digestion. In this study, we evaluated the impact of three plant enzymes (papain, bromelain and ficin) in the manufacture of whey protein hydrolysates with varying level of pH, enzyme-to-substrate ratio and time of hydrolysis, based on a central composite design, to determine the degree of hydrolysis and antihypertensive properties. Hydrolysates made on laboratory scales showed great variation in the type of enzyme used, their concentrations and the pH level of hydrolysis. However, low degrees of hydrolysis in papain and bromelain treatments were associated with increased antihypertensive properties, when compared to ficin. Simulated gastrointestinal digestion performed for selected hydrolysates showed an increase in antihypertensive properties of hydrolysates made with papain and bromelain, which was probably caused by further release of peptides. Several peptides with reported antihypertensive properties were found in all treatments. These results suggest plant enzymes used in this study can be suitable candidates to develop ingredients with bioactive properties.

Changes in the chemical and in-vitro antihypertensive properties of sweet whey obtained from miniature fresh, Chanco and Gouda-style model cheeses.

This Technical Research Communication evaluated the influence of various cheese manufacture methods on the composition and in vitro antihypertensive activity of sweet whey samples obtained from miniature models for fresh, Chanco and Gouda-style cheese processing using bulk-tank milks throughout a year. Raw milks from morning milking were standardized, pasteurized and used to obtain sweet whey using cheesemaking protocols for each variety on 200 g scale, as well the use of whey dilution at levels of 0, 15, 30 and 45% in Chanco and Gouda-style making. The composition of sweet whey obtained within each cheesemaking variety was similar among different timepoints of the year (P > 0.05), which was attributed to similar composition of milks and the use standardized cheesemaking protocols used for this study. As expected, the use of whey dilution led to sweet whey samples with reduced levels of total solids (P < 0.05), but they exhibited an improvement of the in vitro antihypertensive properties, which may be attributed to the formation of low-molecular weight bioactive peptides due to increased cheese making times. The results of this study suggest that modifying cheese manufacture protocols may have a direct impact on the bioactive properties of sweet whey. Future work will be required to identify and evaluate the feasibility to purify bioactive peptides obtained from sweet whey.