TY - JOUR
T1 - Purification and identification of an angiotensin I converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera littoralis
AU - Vercruysse, Lieselot
AU - Smagghe, Guy
AU - Matsui, Toshiro
AU - Van Camp, John
N1 - Funding Information:
This research is supported by a PhD grant for Lieselot Vercruysse from the Institute for the Promotion of Innovation by Science and Technology in Flanders [IWT].
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2008/8
Y1 - 2008/8
N2 - 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.
AB - 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.
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U2 - 10.1016/j.procbio.2008.04.014
DO - 10.1016/j.procbio.2008.04.014
M3 - Article
AN - SCOPUS:46849108707
SN - 0032-9592
VL - 43
SP - 900
EP - 904
JO - Process Biochemistry
JF - Process Biochemistry
IS - 8
ER -