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

Paper ID Volume ID Publish Year Pages File Format Full-Text
35541 45094 2008 5 PDF Available
Title
Purification and identification of an angiotensin I converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera littoralis
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.

Keywords
ACE inhibitory peptide; Insect; Gastrointestinal digestion; Ala-Val-Phe; Purification; Identification
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Purification and identification of an angiotensin I converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera littoralis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 8, August 2008, Pages 900–904
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us