Bovine casein solution was hydrolysed by trypsin for 4 h at a ratio of 1:100. Throughout the experiment, the solution temperature and pH were maintained at 37°C and 7.5, respectively.
AbstractNowadays, the need for new dietary containing some bioactive peptides with specific amino acid sequences increased to express biological functions. We investigated the hypocholesterolemic effect and ACE-inhibiting activity of bovine casein hydrolysates with different molecular weights. The bovine casein was hydrolysed with trypsin for different amounts of time to release bioactive peptides from the casein. Then, crude casein hydrolysate was ultrafiltered using membranes with two different molecular-weight cut offs (1 kDa and 10k Da) to determine the hypocholesterolemic effects and ACE-inhibiting activities of peptides with different molecular weights. The results showed that a higher level of hydrolysis (more active bioactive peptides) was associated with greater hypocholesterolemic and ACE-inhibiting effects in all the tested samples. The unhydrolysed crude casein reduced the cholesterol level in orthophthaldialdehyde (OPA) assays by 39.5%, while the 10 kDa and 1 kDa permeates of casein hydrolysed with trypsin for 4 h reduced the cholesterol level by 50.7 and 69.6%, respectively. The unhydrolysed crude casein and the 10 kDa and 1 kDa permeates of casein hydrolysed by trypsin for 4 h inhibited ACE activity by 18.9%, 29.7%, and 51.4%, respectively.