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Angiotensin I-converting enzyme inhibitory peptides from the hydrolysis of Pacific hake fillets by commerical protease Cinq-Mars, Crystal Dawn


In addition to modifications of diet and lifestyle, angiotensin I-converting enzyme (ACE) inhibitory prescription drugs have been conventionally used to control high blood pressure. Recently, protein hydrolysates, mainly those from milk and fish sources, have been shown to exhibit ACE-inhibitory activity, the most potent of which are now being marketed as nutraceutical alternatives for treatment of hypertension. In this study, Pacific hake (Merluccius productus) fillet was investigated as a source of ACE-inhibitory peptides. Specifically, the objectives were to assess the effects of (1) hydrolysis conditions, (2) raw material variability, (3) ultrafiltration separation, (4) simulated gastrointestinal digestion, and (5) peptide-ACE preincubation on hydrolysate ACE-inhibitory activity in vitro to establish if further study of antihypertensive efficacy in vivo is warranted. Using Protamex® commercial protease according to a Response Surface Methodology (RSM) Central Composite Design, hydrolysis time and enzyme-to-substrate ratio factors were found to be the most significant predictors of ACE-inhibitory activity (P0.05). ACE-inhibitory activity of hydrolysates produced from fish of different catch months and Kudoa infections did not differ significantly (P>0.05). Ultrafiltration of hydrolysate to

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