Formation of an interprotein network in gluten implies three fundamental events: 1) solvation of gluten proteins; 2) mechanical deformation of the solvated protein; 3) stabilization of a 3-D interprotein network through disulfide exchange reactions and rearrangement of hydrophobic patches upon drying/cooking. This report presents some novel approaches for addressing the molecular determinants of the individual steps listed above that were studied in flours of different strength and in various types of semolina. Among the novel tools developed for these purposes, focus will be placed on 1) spectroscopic techniques making it possible to address water distribution and to describe the interaction of water with biological polymers in flour, in semolina, and in raw and cooked pasta products; 2) the significance of intrinsic fluorescence and of noncovalent fluorescent probes to monitor structural rearrangements in proteins at all stages of the various processes; 3) the combined use of proteomics techniques (2D-electrophoresis) and of fluorescent thiol-labeling agents for mapping the free thiol content in flour and semolina having different properties; and 4) the application of selective protein solubilization and of appropriate labeling methods for understanding the molecular events involving thiols and disulfides on specific protein components during development of the interprotein network. Selected examples of the combined use of these methodologies for characterization of starting materials and of finished products will be presented and discussed, also in terms of the possible implementation of some of these protocols for predictive purposes.

Mapping the molecular determinants of inter-protein network formation in gluten

Marengo M;
2011-01-01

Abstract

Formation of an interprotein network in gluten implies three fundamental events: 1) solvation of gluten proteins; 2) mechanical deformation of the solvated protein; 3) stabilization of a 3-D interprotein network through disulfide exchange reactions and rearrangement of hydrophobic patches upon drying/cooking. This report presents some novel approaches for addressing the molecular determinants of the individual steps listed above that were studied in flours of different strength and in various types of semolina. Among the novel tools developed for these purposes, focus will be placed on 1) spectroscopic techniques making it possible to address water distribution and to describe the interaction of water with biological polymers in flour, in semolina, and in raw and cooked pasta products; 2) the significance of intrinsic fluorescence and of noncovalent fluorescent probes to monitor structural rearrangements in proteins at all stages of the various processes; 3) the combined use of proteomics techniques (2D-electrophoresis) and of fluorescent thiol-labeling agents for mapping the free thiol content in flour and semolina having different properties; and 4) the application of selective protein solubilization and of appropriate labeling methods for understanding the molecular events involving thiols and disulfides on specific protein components during development of the interprotein network. Selected examples of the combined use of these methodologies for characterization of starting materials and of finished products will be presented and discussed, also in terms of the possible implementation of some of these protocols for predictive purposes.
2011
AACC International Annual Meeting 2011
Palm Springs, California, USA
16-19 October 2011
56
supplement
A11
A11
Bonomi F; Marengo M; Ragg E; Seetharaman K; Pagani M; Iametti S
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/1732460
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact