Dipeptidyl peptidase-IV, α-amylase, and angiotensin I converting enzyme inhibitory properties of novel camel skin gelatin hydrolysates

In-vitro antidiabetic and antihypertensive properties of novel camel skin gelatin hydrolysates (CSGHs) were reported for the first time. Effect of different proteolytic enzymes, time of hydrolysis and enzyme: substrate (E/S) ratio on the bioactive (antidiabetic and antihypertensive) properties was explored. Results revealed that CSGHs exhibited highly potent inhibitory activity against dipeptidyl peptidase-IV (DPP-IV), pancreatic α-amylase (PA) and angiotensin-I converting enzyme (ACE) compared to non-hydrolyzed camel skin gelatin. All three enzyme combinations used produced highly potent PA inhibitory hydrolysates while for DPP-IV inhibitory property, protease and alcalase-protease (A/P) in combination produced more potent hydrolysates than alcalase generated hydrolysates. Moreover, alcalase and protease generated hydrolysates were highly active in inhibiting ACE activity in comparison to their combination (AP) (P < 0.05). Overall, no significant effect of E/S ratio and time of hydrolysis on production of DPP-IV, PA and ACE inhibitory peptides were observed. These findings suggest that both enzymes i.e. alcalase and protease alone or in combination were capable of producing camel skin gelatin hydrolysates with highly potent antidiabetic and antihypertensive properties. The present study presents the first report on the production of camel skin gelatin hydrolysates with strong in-vitro antidiabetic and antihypertensive potential. Future studies should be directed to identify the sequence of peptides responsibe for antidiabetic and antihypertensive activities.