High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins Running title: HP promotes the release of bioactive peptides from lentil proteins

*Manuscript Click here to view linked References 2 ABSTRACT 1 Angiotensin I converting enzyme (ACE) inhibitory and antioxidant peptides are receiving attention 2 due to their beneficial effects in the prevention/treatment of hypertension. The objective was to 3 explore the effect of high hydrostatic pressure (HP) on proteolysis by different proteases and the 4 release of bioactive peptides from lentil proteins. Pressurisation (100-300 MPa) enhanced the 5 hydrolytic efficiency of Protamex, Savinase and Corolase 7089 compared to Alcalase. Proteolysis at 6 300 MPa led to a complete degradation of lentil proteins and increased peptide (<3 kDa) 7 concentration by all enzymes. Proteolysis at 300 MPa by Savinase gave rise to lentil hydrolysates 8 (S300) with the highest ACE-inhibitory and antioxidant activities that were retained upon in vitro 9 gastrointestinal digestion. The peptides responsible for the multifunctional properties of S300 10 hydrolysate were identified as different fragments from storage proteins and the allergen Len c 1. 11 These results support the potential of HP as a technology for the cost-effective production of 12 bioactive peptides from lentil proteins during enzymatic proteolysis. 13