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Mass Spectrometry Characterization of the SDS-PAGE Protein Profile of Legumins and Vicilins from Chickpea Seed

ABSTRACT:

SUBMITTER: Di Francesco A

PROVIDER: S-EPMC10969193 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature

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An in-depth Mass Spectrometry Characterization of the SDS-PAGE Protein Profile of Legumins and Vicilins from Chickpea Seed

Project description:Chickpea (Cicer arietinum L.) seed proteins show a lot of functional properties leading this leg-ume an interesting component for the development of protein-enriched foods. However, both in-depth proteomic investigation and structural characterization of chickpea proteins seed are still lacking. In this paper we report a detailed characterization of chickpea seed protein fraction by means SDS-PAGE, in-gel protein digestion, high-resolution mass spectrometry, and database searching. By this approach twenty SDS gel bands were cut and analysed. While the majority of bands and the identified peptides were related to vicilin and legumin storage proteins, also metabolic functional proteins were detected. Legumins, as expected, were revealed at 45÷65 kDa, as whole subunits with the α- and β-chains linked together by a disulphide bond, but also at lower mass ranges (α- and β-chains migrating alone). Similarly, but not expected, also the vi-cilins were spread along the mass region between 65 and 23 kDa, with some of them identified in several bands. In-depth MS structural characterization allowed to determine that, although chickpea vicilins were always described as proteins lacking of cysteine residues, they contain this amino acid residue. Moreover, similarly to legumins, these storage proteins are firstly syn-thesized as pre-propolypeptides (Mr 50÷80 kDa), that may undergo to proteolytic steps that cut not only the signal peptides but also produce different subunits having lower molecular masses. Overall, about 360 different proteins specific of the Cicer arietinum L. species were identified and characterized, a result that up to date represents the most detailed description of seed’s proteome of this legume.

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