Lipid transfer proteins (LTPs) are ubiquitous plant lipidbinding proteins that have been associated with multiple developmental and stress responses. Although LTPs typically bind fatty acids and fatty acid derivatives in a non-covalent way, studies on the LTPs of barley seeds have identified an abundantly occurring covalently modified form, LTP1b, the lipid ligand of which has resisted clarification. In the present study, this adduct was identified as the ␣-ketol 9-hydroxy-10-oxo-12(Z)-octadecenoic acid. Further studies on the formation of LTP1b demonstrated that the ligand was introduced by nucleophilic attack of the free carboxylate group of the Asp-7 residue of the protein at carbon-9 of the allene oxide fatty acid 9(S),10-epoxy-10,12(Z)-octadecadienoic acid. This reactive oxylipin was produced in barley seeds by oxygenation of linoleic acid by 9-lipoxygenase followed by dehydration of the resulting hydroperoxide by allene oxide synthase. The generation of protein-oxylipin adducts represents a new function for plant allene oxide synthases, enzymes that have earlier been implicated mainly in the biosynthesis of the jasmonate family of plant hormones. Additionally, the LTP-allene oxide synthase interaction opens new perspectives regarding the roles of LTPs in the signaling of plant defense and development.

Apple pieces were vacuum-impregnated with either a pectin methylesterase (PME) and calcium solution or with water prior to pasteurization. Pasteurized apple pieces impregnated with PME and calcium showed a significantly higher firmness. Moreover, solid state (13)C NMR spectroscopy of apple cell wall residues revealed an increase of their molecular rigidity. Exogenous PME addition involved a decrease from 82% to 45% of apple pectin degree of methyl-esterification. Microscopic observations of apple slices immunolabelled with antibodies specific for pectins showed that (i) demethyl-esterification was more intense in the cell wall region lining intercellular spaces (demonstrating a key role for these intercellular channels in the enzyme penetration in the tissue during vacuum-infusion) and that (ii) the number of calcium-dimerized deesterified homogalacturonan chains increased. The results corroborate the hypothesis that vacuum-impregnated PME action liberates free carboxyl groups along pectin chains that could interact with calcium, increasing the rigidity of pectins and finally the mechanical rigidity of apple tissue.

In order to determine the relationship between molecular structure of wheat bread dough, its mechanical properties, total and local bread expansion during baking and final bread quality, different methods (rheological, nuclear magnetic resonance, magnetic resonance imaging and general bread characterisation) were employed. The study was extended on wheat dough with starch modified by octenyl succinic anhydride (OSA) in order to generalise the results. The interest of investigating multi-scale changes occurring in dough at different phases of baking process by considering overall results was demonstrated. It was found that OSA starch improved the baking performance during the first phase of baking. This feature was due to a higher absorption of water by OSA starch granules occurring at temperatures below that of starch gelatinization, as confirmed by NMR, and consecutive higher resistance to deformation for OSA dough in this temperature range (20-60°C). This was explained by a delayed collapse of cell walls in the bottom of the OSA dough. In the second phase of baking (60-80°C), the mechanism of shrinkage reduced the volume gained by OSA dough during the first phase of baking due to higher rigidity of OSA dough and its higher resistance to deformation. MRI monitoring of the inflation during baking made it possible to distinguish the qualities and defaults coming from the addition of OSA starch as well as to suggest the possible mechanisms at the origin of such dough behaviour.