ACE inhibitory activity in enzymatic hydrolysates of insect protein.
In this paper, ACE inhibitory activity in insect protein hydrolyzed by various enzymes (gastrointestinal proteases, alcalase, and thermolysin) is reported for the first time. Four insects of different insect orders were tested: Spodoptera littoralis (Lepidoptera), Bombyx mori (Lepidoptera), Schistocerca gregaria (Orthoptera), and Bombus terrestris (Hymenoptera). ACE inhibitory activity was measured by two different methods: a spectrophotometric method using FAPGG (2-furanacryloyl-phenylalanyl-glycyl-glycine) as substrate, and an HPLC method using dansyltriglycine (DTG) as substrate. Hydrolysis of the insect protein resulted in an increased ACE inhibitory activity. Overall, the highest ACE inhibitory activity was obtained after gastrointestinal digestion. These results suggest a role for insect protein as antihypertensive component in functional foods and nutraceuticals. Furthermore, the ACE inhibitory activity differed according to the method used. As a consequence, there is a need to standardize methodologies to evaluate ACE inhibitory activity.
Vercruysse
Lieselot
L
Laboratory of Agrozoology, Department of Crop Protection, and Laboratory of Food Science, Faculty of Bioscience Engineering, Ghent University, Belgium. lieselot.vercruysse@ugent.be
Smagghe
Guy
G
Herregods
Griet
G
Van Camp
John
J
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis*; D000818:Animals; D012831:Bombyx / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D006110:Grasshoppers / Q000737:chemistry; D006868:Hydrolysis; D006927:Hymenoptera / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000378:metabolism; D018411:Spodoptera / Q000737:chemistry; D013381:Subtilisins / Q000378:metabolism; D013820:Thermolysin / Q000378:metabolism
D000806:Angiotensin-Converting Enzyme Inhibitors; D019476:Insect Proteins; D010447:Peptide Hydrolases; D013381:Subtilisins; D013820:Thermolysin