Purification and identification of an angiotensin I converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera littoralis

Lieselot Vercruysse, Guy Smagghe, Toshiro Matsui, John Van Camp

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Enzymatic hydrolysis of the protein from an edible insect species, the cotton leafworm Spodoptera littoralis (Lepidoptera) leads to the release of angiotensin I converting enzyme (ACE) inhibitory peptides. The subsequent hydrolysis with pepsin, trypsin and α-chymotrypsin was designed to simulate the human gastrointestinal digestion process. After fractionation of this hydrolysate using consecutive chromatographic techniques, including size exclusion chromatography and reverse-phase high-performance liquid chromatography, a new ACE inhibitory tripeptide was identified. The amino acid sequence of the tripeptide was determined as Ala-Val-Phe and the in vitro ACE inhibitory activity assay revealed an IC50 value of 2123 μM.

Original languageEnglish
Pages (from-to)900-904
Number of pages5
JournalProcess Biochemistry
Volume43
Issue number8
DOIs
Publication statusPublished - Aug 1 2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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