Optimizing angiotensin I-converting enzyme inhibitory activity of Pacific hake (Merluccius productus) fillet hydrolysate using response surface methodology and ultrafiltration.
The in vitro angiotensin I-converting enyzme (ACE) inhibitory activity of Pacific hake hydrolysates was investigated as a function of hydrolysis conditions, starting material variability, and ultrafiltration. Hake fillets were hydrolyzed using Protamex protease under various conditions of pH, hydrolysis time, and enzyme-to-substrate ratio (% E/S) according to a response surface methodology (RSM) central composite design. The hydrolysate produced at pH 6.5, 125 min, and 3.0% E/S had an IC 50 of 165 +/- 9 microg of total solids/mL. ACE-inhibitory activity was not significantly different (P < 0.05) for hydrolysates produced using higher time-enzyme combinations within the model or from fish of different catches. Ultrafiltration (10 kDa molecular mass cutoff) resulted in an IC50 value of 44 +/- 7 microg of peptides/mL, 2.5 times more potent than the commercial product PeptACE Peptides (IC50 = 114 +/- 8 microg of peptides/mL). These results suggest that hydrolysates prepared with minimal fractionation from Pacific hake, an undervalued fish, may be a commercially competitive source of ACE-inhibitory peptides.
Cinq-Mars
Crystal D
CD
Food, Nutrition, and Health Program, Faculty of Land and Food Systems, 2205 East Mall, The University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4.
Li-Chan
Eunice C Y
EC
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000818:Animals; D029941:Fish Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D048388:Gadiformes; D006868:Hydrolysis; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D014462:Ultrafiltration
D000806:Angiotensin-Converting Enzyme Inhibitors; D029941:Fish Proteins; D010455:Peptides