Applications of mass spectrometry to food proteins and peptides

The application of mass spectrometry (MS) to large biomolecules has been re volutionized in the past decade with the development of electrospray ioniza tion (ESI) and matrix-assisted lasts desorption/ionization (MALDI) techniqu es. ESI and MALDI permit solvent evaporation and sublimation of large biomo lecules into the gaseous phase, respectively. The coupling of ESI or MALDI to an appropriate mass spectrometer has allowed the determination of accura te molecular mass and the detection of chemical modification at high sensit ivity (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, pro tein conformations (native, denatured, folding intermediates), protein fold ing/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. (C) 2000 Elsevier Science B. V. All rights reserved.