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Food Chem ; 239: 1027-1036, 2018 Jan 15.
Article in English | MEDLINE | ID: mdl-28873519

ABSTRACT

Soluble proteins were extracted from common wheat flour obtained from nine cultivars of different qualities and were analyzed by nanoUPLC and Ultra Definition Mass Spectrometry (UDMSE) label-free quantitative approach. Collectively, 5894 proteins were identified and quantified with 8 peptides/protein. A total of 414 proteins were found differentially expressed with 85% proteins not yet described in the literature, according to their biological function. Quality-related proteins, such as puroindolines and chaperones, notably involved in the gluten-protein folding process, were up-regulated in superior (SP) and medium (MD) flours qualities and down-regulated in the low (LW) ones. Domains related to the chaperones activity were also found up-regulated in SP and MD and down-regulated in LW. In this work, nanoUPLC-UDMSE analysis was effective to identify and quantify metabolic proteins, allowing a clear distinction of the wheat flours and providing new perspectives for evaluating the technological quality based on the low abundant proteins of wheat endosperm.


Subject(s)
Albumins/analysis , Globulins/analysis , Triticum , Chromatography, High Pressure Liquid , Flour , Mass Spectrometry , Plant Proteins
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