Identification of antioxidant peptides of hen egg-white lysozyme and evaluation of inhibition of lipid peroxidation and cytotoxicity in the Zebrafish model
2016
Carrillo, W. | Gómez-Ruiz, José Ángel | Miralles, Beatriz | Ramos González, María Mercedes | Recio, Isidra | Ministerio de Economía y Competitividad (España) | Comunidad de Madrid | Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina) | Universidad Técnica de Ambato | Universidad Nacional de Río Negro
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.
显示更多 [+] 显示较少 [-]This study was supported with Project Number AGL2015-66886-R of Instituto de Investigación en Ciencias de la Alimentación, CIAL (CSIC-UAM), Madrid, Spain, and project number CPU-1373-2014-UTA of Universidad Técnica de Ambato, Ecuador/Universidad Nacional Rio Negro, Argentina. Carrillo W. thanks Comunidad Autónoma de Madrid for the research contract to complete his PhD. Daniel Alejandro Barrio is member of the Carrera del Investigador, CONICET, Argentina.
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