Potential ACE-inhibitory activity and nanoLC-MS/MS sequencing of peptides derived from aflatoxin contaminated peanut meal

Autor:	Timothy H. Sanders, Brittany L. White, Jack P. Davis
Rok vydání:	2014
Předmět:	chemistry.chemical_classification Aflatoxin Chromatography Protease Chemistry medicine.medical_treatment Size-exclusion chromatography Ultrafiltration Hydrolysate Hydrolysis medicine Storage protein IC50 Food Science
Zdroj:	LWT - Food Science and Technology. 56:537-542
ISSN:	0023-6438
Popis:	Our lab has developed a process for sequestering aflatoxin from contaminated peanut meal (PM) using commercial bentonite clays while protein is simultaneously extracted and hydrolyzed by a commercial protease. The objectives of this study were to sequence generated peptides and evaluate their potential ACE-inhibitory properties. Aflatoxin in the unprocessed PM was 610 μg kg−1 compared to 9.7 μg kg−1 on a dry weight basis in the 120 min hydrolysate. This hydrolysate displayed significant ACE-inhibitory activity with an IC50 of 295.1 μg mL−1. Ultrafiltration and size exclusion chromatography (SEC) improved the ACE-inhibitory properties, with the SEC fraction containing the smallest peptides having an IC50 = 44.4 μg mL−1. Additionally, 271 unique peptides were identified by nanoLC-MS/MS, of which 147 belonged to major seed storage proteins. This advanced characterization data will ultimately allow for more efficient production of hydrolysates with ACE-inhibitory activity or other bioactivities of interest from PM.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::325b12eb1fa809015903e08c543998b3 https://doi.org/10.1016/j.lwt.2013.11.039 Zobrazit plný text záznamu Full Text from ScienceDirect