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Identification of active peptides from backbones of Nemipterus japonicus and Exocoetus volitans by electrospray ionisation–mass spectrometry
Author(s) -
Shabeena Yousuf N.,
Nazeer Rasool Abdul
Publication year - 2011
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2011.02691.x
Subject(s) - hydrolysate , chemistry , amino acid , trypsin , peptide , chromatography , electrospray ionization , proteases , pepsin , peptide sequence , hydrolysis , electrospray , biochemistry , mass spectrometry , enzyme , gene
Summary In our present investigation, Nemipterus japonicus and Exocoetus volitans backbone protein were hydrolysed by proteases like trypsin and pepsin, respectively. The protein hydrolysates were purified by different chromatographic methods, and the resulted purified peptides were analysed for their amino acid sequences by electrospray ionisation–MS/MS. The analysis of peptides showed sequences as Gly‐His‐Met‐Ser (451.8 Da) and Leu‐Glu‐Val‐Lys‐Pro (596.9 Da) for N. japonicus and E. volitans muscle, respectively. The presence of hydrophobic amino acids contributes more to the antioxidant activities of peptides than other amino acids. Moreover, sequence of amino acids in peptides plays an important role in their antioxidant activities.