info:eu-repo/semantics/article
Identification of antioxidant peptides of hen egg-white lysozyme and evaluation of inhibition of lipid peroxidation and cytotoxicity in the Zebrafish model
Fecha
2016-04-01Registro en:
Carrillo, Wilman; Gómez Ruiz, J. A.; Miralles, B.; Ramos, M.; Barrio, Daniel Alejandro; et al.; Identification of antioxidant peptides of hen egg-white lysozyme and evaluation of inhibition of lipid peroxidation and cytotoxicity in the Zebrafish model; Springer; European Food Research and Technology; 242; 10; 1-4-2016; 1777-1785
1438-2377
1438-2385
CONICET Digital
CONICET
Autor
Carrillo, Wilman
Gómez Ruiz, J. A.
Miralles, B.
Ramos, M.
Barrio, Daniel Alejandro
Recio, I.
Resumen
Hen egg lysozyme was hydrolyzed with pepsin in situ on a cation-exchange column to isolate antioxidant peptides. The most cationic fraction was eluted with 1 M NaCl. Five positively charged peptides f(109–119) VAWRNRCKGTD, f(111–119) WRNRCKGTD, f(122–129) AWIRGCRL, f(123–129) WIRGCRL and f(124–129) IRGCRL were identified using tandem mass spectrometry. Using ORAC-FL , all five peptides presented antioxidant activity with values of (1970, 3123, 2743, 2393 and 0.313 µmol Trolox/µmol peptide), respectively. Using method TBARS in Zebrafish larvae, all five synthetic peptides were found to efficiently inhibit lipid peroxidation (36.8, 51.6, 55.56, 63.2, 61.0 % inhibition of lipid peroxidation), respectively. None of the five peptides were toxic in Zebrafish eggs and larvae at concentrations lower than 50 µg/ml. Concentrations higher than 50 µg/ml were toxic for both Zebrafish eggs and larvae.