Applications of mass spectrometry to food proteins and peptides.
The application of mass spectrometry (MS) to large biomolecules has been revolutionized in the past decade with the development of electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) techniques. ESI and MALDI permit solvent evaporation and sublimation of large biomolecules into the gaseous phase, respectively. The coupling of ESI or MALDI to an appropriate mass spectrometer has allowed the determination of accurate molecular mass and the detection of chemical modification at high sensitivity (picomole to femtomole). The interface of mass spectrometry hardware with computers and new extended mass spectrometric methods has resulted in the use of MS for protein sequencing, post-translational modifications, protein conformations (native, denatured, folding intermediates), protein folding/unfolding, and protein-protein or protein-ligand interactions. In this review, applications of MS, particularly ESI-MS and MALDI time-of-flight MS, to food proteins and peptides are described.
Alomirah
H F
HF
Department of Food Science and Agricultural Chemistry, McGill University, Ste Anne de Bellevue, Montreal, Canada.
Alli
I
I
Konishi
Y
Y
D000097:Acetonitriles / Q000032:analysis* / Q000737:chemistry; D000818:Animals; D005504:Food Analysis; D013058:Mass Spectrometry / Q000379:methods*; D010455:Peptides / Q000032:analysis*; D010944:Plants / Q000737:chemistry; D011506:Proteins / Q000032:analysis*
D000097:Acetonitriles; D010455:Peptides; D011506:Proteins; C419311:hydroxy-3-phenoxybenzeneacetonitrile