Mass spectrometry in the characterization of cereal seed proteins

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Eur. J. Mass Spectrom. DOI: 10.1255/ejms.609

Mass spectrometry in the characterization of cereal seed proteins

Vincenzo Cunsolo, Salvatore Foti,^* Rosaria Saletti
Dipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria, 6, I-95125 Catania, Italy

ABSTRACT:

In less then a decade, applications of MALDI and ESI mass spectrometry to the investigation of prolamins have rapidly evolved from the measurements of the molecular mass of isolated proteins to a proteomic approach attempting to characterize the complete protein pattern in the seed. Mass spectrometry is currently making significant contributions to the understanding of the composition and structure of the gluten proteins and, in turn, to the elucidation of structure-function relationships. Results obtained using mass spectrometry, including determination of the molecular masses of prolamins, direct verification of gene-derived sequences, determination of the number of cysteine residues and localization of disulphide bonds, investigation of the gluten toxicity for coeliac patients, qualitative and quantitative determination of gliadins in food and determination of the protein pattern and its modification during seed maturation by proteomic approaches, are summarized here, to illustrate current trends and individuate possible future perspectives.

Keywords: prolamins, MALDI-TOF-MS, ESI-MS

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