Sourice Sophie, Nisole Audrey, Guéguen Jacques, Popineau Yves, Elmorjani Khalil
Unité de Recherche sur les Protéines végétales et leurs interactions INRA, Rue de la Géraudière, Nantes, France.
Biochem Biophys Res Commun. 2003 Dec 26;312(4):989-96. doi: 10.1016/j.bbrc.2003.11.028.
Primary structures of wheat prolamins contain repetitive domains involved in the mechanical properties of gluten. In order to experience the ability of recombinant strictly periodic polypeptides, modelled on a consensus sequence of wheat gliadins (PQQPY)(8) and (PQQPY)(17) (SPR8 and SPR17 polypeptides, respectively), to be formulated in film solutions, their heterologous expression conditions, in batch culture and low cell densities, were optimized to match the high requirements of this process. A convenient and general purification procedure was also devised. Moreover, FTIR-ATR characterizations indicated that these periodic polypeptides prepared as hydrated doughy state and dried have the tendency to form a protein network through intermolecular beta-sheets, strongly maintained by hydrogen bonds. Accordingly, these recombinant polypeptides are assumed to be a suitable candidate for potential application.
