Journal
FOOD CHEMISTRY
Volume 155, Issue -, Pages 132-139Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.01.032
Keywords
Electrophoresis; Globulins; Grape seed; Mass spectrometry; Seed proteins
Ask authors/readers for more resources
In the present study, grape (Vitis vinifera L.) seed endosperm proteins were characterized after sequential fractionation, according to a modified Osborne procedure. The salt-soluble fraction (albumins and globulins) comprised the majority (58.4%) of the total extracted protein. The protein fractions analysed by SDS-PAGE showed similar bands, indicating different solubility of the same protein components. SDS-PAGE in non-reducing and reducing conditions revealed the polypeptide composition of the protein bands. The main polypeptides, which were similar in all the grape varieties analysed, were identified by LC-MS/MS as homologous to the 115 globulin-like seed storage proteins of other plant species, while a monomeric 43 kDa protein presented high homology with the 75 globulins of legume seeds. The results provide new insights about the identity, structure and polypeptide composition of the grape seed storage proteins. (C) 2014 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available