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

• Published in: Marine biotechnology (New York, N.Y.) Vol. 24; no. 5; pp. 882 - 894
• Main Authors: Windarto, Seto, Lee, Meng-Chou, Nursyam, Happy, Hsu, Jue-Liang
• Format: Journal Article
• Language: English
• Published: New York Springer US 01-10-2022; Springer Nature B.V
• Subjects: Acrochaetium; Algae; Angiotensin-converting enzyme inhibitors; Bioactive compounds; Biological activity; Biomedical and Life Sciences; Cation exchange; Cation exchanging; Cations; Chromatography; Chymotrypsin; Engineering; Food; Food availability; Foods; Freshwater & Marine Ecology; Functional foods & nutraceuticals; Hydrolysates; Hypertension; Inhibitors; Life Sciences; Microbiology; Molecular docking; Original Article; Peptides; Proteins; Proteolysis; Proteolytic enzymes; Screening; Zoology; Hypertension; Chymotrypsin; Seaweed; ACE inhibitory peptide; Phycoerythrin
• ISSN: 1436-2228; 1436-2236
• DOI: 10.1007/s10126-022-10152-w

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 α-chymotrypsin. It comes from Phycoerythrin (PE), an abundant protein in a primarily red alga. The peptide VL-9 shows the ACE inhibitory activity with IC
50
value 433.1 ± 1.08 µM. 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.