Smith, Brennan M.2009-08-132009-08-132009-08-13http://hdl.handle.net/2097/1659The biochemical, physical and baking properties of caroubin, the main protein in the carob bean, were characterized. The biochemical properties of caroubin were analyzed using reversed-phase high performance liquid chromatography (RP-HPLC), size exclusion chromatography coupled with multi-angle laser light scattering (SEC-MALS) and micro-fluidics analysis. The physical and baking properties of caroubin were characterized via SE-HPLC, laser scanning confocal microscopy, farinograph mixing, and texture profile analyzer analysis. Using a modified Osborne fractionation method, carob germ flour proteins were found to contain ~32% albumin and globulin and ~68% glutelin with no prolamins detected. When divided into soluble and insoluble protein fractions under non reducing conditions it was found that caroubin contained (~95%) soluble proteins and only (~5%) insoluble proteins. As in wheat, SEC-MALS analysis showed that the insoluble proteins had a greater Mw than the soluble proteins and ranged up to 8x107 Da. These polymeric proteins appeared to play a critical role in protein network formation. Analysis of the physical properties of carob germ protein-maize starch dough showed that the dough’s functionality was dependent on disulfide bonded protein networks, similar to what is found in wheat gluten. When baked into a bread these proteins were shown to have a possible improving affect by decreasing staling in gluten-free breads. This was evident when compared to a gluten-free batter bread, and a wheat bread over a five day period.en-USCarobCarob germglutengluten-freeceliacThesisAgriculture, Food Science and Technology (0359)