Rationale:Authentication of fish is of importance in the view of toxins, allergen warnings and economic fraud control. Traditional methods in the authentication of fish, e.g. morphological, genetic and proteomic analysis, are either at low throughput or at high-cost.
Methods:A high-throughput matrix-assisted laser desorption/ionization time-offlight mass spectrometry (MALDI TOF MS)-based approach was developed to analyze biomaterials from fish skin, and mass spectra from different fish species were compared by chemometric methods to differentiate fish species.Results: A total of 51 fish samples were used to generate more than 150 fingerprinting mass spectra. The fish belonging to the same genus can be identified at species level. A mass spectral database of different fishes can be built as reference for authentication. The analysis can be performed based on micrograms of fish-skin sample and accomplished in 1-3 hours.
Conclusions:The developed strategy holds potential to be applied to fish authentication in the fishing industry and as a scientific method to avoid mislabeling. It has promise to be practically used for fast and effective identification of closely related fish species to guarantee the quality of fishery products to consumers.
A surface molecular transferring strategy is the first to be utilized for the direct analysis of fish samples by mass spectrometry, and it promisingly enables fish authentication in a quick, efficient and easy mode.
The cover image is based on the Research Article Differentiation and Authentication of Fishes at Species Level Through Analysis of Fish Skin by MALDI TOF MS by Hongyan Bi et al., https://doi.org/10.1002/rcm.8474.
Protein phosphorylation,
a post-translational modification of proteins,
is important in biological regulation. The quantity of phosphorylated
proteins is a key requirement for the quality change of animal muscle
foods. In the present study, a new approach to quantify phosphorylated
proteins and/or peptides was developed based on ferric ions (Fe
3+
) and UV/vis spectrometry. This method is proved to be ultra-effective
in discriminating phosphopeptides and non-phosphopeptides with the
assistance of Fe
3+
. The protocol of extracting proteins
with 0.1% trifluoroacetic acid (TFA) solution from animal muscle samples
coupled with Fe
3+
was verified by using an artificial mixture
of peptides with different phosphorylation sites and was successfully
used to characterize the phosphorylation quantity in the samples via
UV/vis spectrometry. A peptide with one phosphorylated site was taken
as a reference standard and successfully utilized for the absolute
quantification of phosphorylated proteins in caprine muscles during
frozen storage and in fish muscle food samples. This present study
paves a new way for the evaluation of phosphorylated protein quantitative
levels in bio-samples.
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