期刊
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
卷 242, 期 10, 页码 1777-1785出版社
SPRINGER
DOI: 10.1007/s00217-016-2677-1
关键词
Lysozyme; Antioxidant activity in Zebrafish larvae; Bioactive peptides; Hydrolyzate; Cation-exchange column; Toxicity in Zebrafish egg
资金
- Instituto de Investigacion en Ciencias de la Alimentacion, CIAL (CSIC-UAM), Madrid, Spain [AGL2015-66886-R]
- Universidad Tecnica de Ambato, Ecuador/Universidad Nacional Rio Negro, Argentina [CPU-1373-2014-UTA]
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 A mu mol Trolox/A mu mol 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 A mu g/ml. Concentrations higher than 50 A mu g/ml were toxic for both Zebrafish eggs and larvae.
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