ACE inhibitory activity in enzymatic hydrolysates of insect protein

J Agric Food Chem. 2005 Jun 29;53(13):5207-11. doi: 10.1021/jf050337q.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / analysis*
  • Animals
  • Bombyx / chemistry
  • Chromatography, High Pressure Liquid
  • Grasshoppers / chemistry
  • Hydrolysis
  • Hymenoptera / chemistry
  • Insect Proteins / chemistry*
  • Peptide Hydrolases / metabolism
  • Spodoptera / chemistry
  • Subtilisins / metabolism
  • Thermolysin / metabolism

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Insect Proteins
  • Peptide Hydrolases
  • Subtilisins
  • Thermolysin