Dimeric Inhibitors of Human Salivary α-Amylase from Emmer (Triticum dicoccon Schrank) Seeds
2007
Fontanini, D. | Capocchi, A. | Muccilli, V. | Saviozzi, F. | Cunsolo, V. | Saletti, R. | Foti, S. | Galleschi, L.
The proteins belonging to the cereal trypsin/α-amylase inhibitor family are abundant water/salt-soluble flour proteins active against α-amylases from several seed parasites and pests and inactive against endogenous α-amylases. Three α-amylase inhibitor families have been described in cereals that vary in size and are differently expressed among Triticeae seeds. The present work investigates the presence of human salivary α-amylase inhibitors in emmer (Triticum dicoccon Schrank) flour. The isolation was obtained by a series of chromatography steps, and the purification progress was monitored through the inhibition of human salivary α-amylase activity. The purified fraction was subjected to protein sequencing by tandem mass spectrometry (MSMS) of the tryptic digests obtained after the sample separation on 2-DE. MSMS data indicated that the emmer α-amylase inhibitory fraction was composed of two newly identified proteins [emmer dimeric inhibitor 1 (EDI-1) and emmer dimeric inhibitor 2 (EDI-2)] sharing very high identity levels with related proteins from Triticum aestivum.
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