First Report of Screening of Novel Angiotensin-I Converting Enzyme Inhibitory Peptides Derived from the Red Alga Acrochaetium sp.

Abstract

ACE inhibitors generated from food proteins have recently become the most well-known subclass of bioactive peptides, and their bio-functionality can be a potential alternative to natural bioactive food components and synthetic drugs. The bioactivities of Acrochaetium sp., the red alga used in this investigation, have never been reported before. Screening of bioactive peptides from Acrochaetium sp. as ACE inhibitors were hydrolyzed with various proteolytic enzymes. Protein hydrolysates were fractionated separately using reversed phased (RP) and strong cation exchange (SCX) chromatography and identified as VGGSDLQAL (VL-9) using alpha-chymotrypsin. It comes from Phycoerythrin (PE), an abundant protein in a primarily red alga. The peptide VL-9 shows the ACE inhibitory activity with IC50 value 433.1 +/- 1.08 mu M. The inhibition pattern showed VL-9 as a non-competitive inhibitor. Molecular docking simulation proved that VL-9 was non-competitive inhibition due to the interaction peptide and ACE was not in the catalytic site. Moreover, VL-9 derived from Acrochaetium sp. is a natural bioactive peptide that is safer and available for food protein; also, the ACE inhibitory peptide derived from Acrochaetium sp. could be the one alternative resource to develop functional food for combating hypertension.