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Título

Identification of antioxidant peptides of hen egg-white lysozyme and evaluation of inhibition of lipid peroxidation and cytotoxicity in the Zebrafish model

AutorCarrillo, W. CSIC ORCID; Gómez-Ruiz, José Ángel CSIC; Miralles, Beatriz CSIC ORCID ; Ramos González, María Mercedes CSIC ; Recio, Isidra CSIC ORCID
Palabras claveLysozyme
Bioactive peptides
Hydrolyzate
Antioxidant activity in Zebrafish larvae
Toxicity in Zebrafish egg
Cation-exchange column
Fecha de publicación2016
EditorSpringer Nature
CitaciónEuropean Food Research and Technology 242(10): 1777-1785 (2016)
ResumenHen 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.
Versión del editorhttps://doi.org/10.1007/s00217-016-2677-1
URIhttp://hdl.handle.net/10261/150277
DOI10.1007/s00217-016-2677-1
Identificadoresdoi: 10.1007/s00217-016-2677-1
e-issn: 1438-2385
issn: 1438-2377
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