RT info:eu-repo/semantics/article
T1 Revalorization of a peach (Prunus persica (L.) Batsch) byproduct: Extraction and characterization of ACE-inhibitory peptides from peach stones
A1 Vásquez Villanueva, Romy Ángela
A1 Marina Alegre, María Luisa
A1 García López, María Concepción
K1 Peach
K1 Seed
K1 Peptides
K1 ACE-inhibitor
K1 De novo sequencing
K1 Ciencia
K1 Química
K1 Science
K1 Chemistry
AB The value-added use of peach stone for production of a high protein product was investigated. Different parameters were optimized in order to obtain the highest protein yield in the extraction of peach seed proteins. Optimal conditions enabled the extraction of 43 g of protein per 100 g of dried and defatted milled seeds. Different enzymes and parameters were also tried in order to obtain the highest hydrolysis degree in the digestion of this peach seed protein isolate. Thermolysin was the enzyme that yielded the extract with the highest ACE-inhibition capability. After ultrafiltration through different molecular weight cut-off filters, potential antihypertensive peptides remained in the fraction below 3 kDa. Three different peptides (LYSPH, LYTPH, and HLLP) resisting simulated gastrointestinal digestion and ACE activity and demonstrating antihypertensive in vitro capacity were identified by HPLC-MS/MS. This is the first time that potential antihypertensive peptides have been isolated from peach stones.
PB Elsevier
SN 1756-4646
YR 2015
FD 2015
LK http://hdl.handle.net/10017/24604
UL http://hdl.handle.net/10017/24604
LA eng
DS MINDS@UW
RD 25-abr-2024