http://www.cnr.it/ontology/cnr/individuo/prodotto/ID46627
Reliable detection of milk allergens in food using a high-resolution, stand-alone mass spectrometer. (Articolo in rivista)
- Type
- Label
- Reliable detection of milk allergens in food using a high-resolution, stand-alone mass spectrometer. (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Alternative label
Monaci L., Losito I., Palmisano F., Visconti A. (2011)
Reliable detection of milk allergens in food using a high-resolution, stand-alone mass spectrometer.
in Journal of AOAC International
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Monaci L., Losito I., Palmisano F., Visconti A. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- ISPA-CNR IT, University of Bari (literal)
- Titolo
- Reliable detection of milk allergens in food using a high-resolution, stand-alone mass spectrometer. (literal)
- Abstract
- Reliable methods are needed for detection of
allergenic milk proteins in complex food matrixes.
The feasibility of an LC/high-resolution MS method
for the analysis of milk proteins in a thermally
processed model food (incurred cookies) and in
white wine spiked, respectively, with milk powder
and caseinate is described. Detection of milk
proteins was based on the identification of unique
peptides in the tryptic digests of cookie/wine
extracts using an RP-HPLC separation coupled to
an Exactive(TM) nonhybrid mass spectrometer using
Orbitrap technology. The extremely high mass
accuracy and resolution provided by the Orbitrap
analyzer allowed a fast preliminary identification of
four previously proposed peptide markers of
caseins using only accurate values of the m/z of
their ions. No interference was observed, despite
the complexity of the analyzed matrixes. Moreover,
the availability of a high- energy, collisionally
activated dissociation cell integrated in the mass
spectrometer enabled acquisition of peptide
MS/MS-like spectra through post-source
fragmentation. Confirmation of peptide marker
identity could then be achieved by a comparison
between experimental and predicted product ions.
The described method shows the great potential of
Orbitrap MS as a reliable technique in the field of
protein allergen detection once the peptide
markers are identified. (literal)
- Prodotto di
- Autore CNR
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