Isolation and Identification of Flavor Peptides in Cultured Puffer Fish (Takifugu obscurus)
Article
Figures
Metrics
Preview PDF
Reference
Related
Cited by
Materials
Abstract:
The aim of this study was to isolate and study the structural properties of flavor peptides from raw, cultured puffer fish muscle. Three fractions (0-F1, 0-F2, and 0-F3) were obtained from an aqueous extraction of cultured puffer fish (Takifugu obscurus) muscle by Sephadex G-15 gel filtration chromatography. Using sensory evaluation analysis and an electronic tongue, it was found that fraction 0-F1 could elicit umami and kokumi tastes. Further isolation of fraction 0-F1 components was performed using reverse-phase high-performance liquid chromatography (RP-HPLC) to yield two subfractions 0-F1-1 and 0-F1-2. The electronic tongue showed that subfraction 0-F1-1 could elicit a relatively strong umami taste. The amino acid sequence of subfraction 0-F1-1 isolated by RP-HPLC was identified using matrix-assisted laser desorption-ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and the structure of this new flavor peptide was Pro-A-Ala-B Met*-Cys-Arg (810.9046 Da, where A and B are amino acid codes; Met* is oxidative methionine). Although this peptide contained a large number of hydrophobic amino acids, it did not have a bitter taste, and rather a thick and strong taste. Hydrophilic amino acid residue Cys might be the key factor contributing to the kokumi taste of this peptide.
