Composition and molecular weight distribution of carob germ protein fractions.

Biochemical properties of carob germ proteins were analyzed using a combination of selective extraction, reversed-phase high-performance liquid chromatography (RP-HPLC), size exclusion chromatography (SEC) coupled with multiangle laser light scattering (SEC-MALS), and electrophoretic analysis. Using a modified Osborne extraction procedure, carob germ flour proteins were found to contain approximately 32% albumin and globulin and approximately 68% glutelin with no prolamins detected. The albumin and globulin fraction was found to contain low amounts of disulfide-bonded polymers with relatively low M(w) ranging up to 5 x 10(6) Da. The glutelin fraction, however, was found to contain large amounts of high molecular weight disulfide-bonded polymers with M(w) up to 8 x 10(7) Da. When extracted under nonreducing conditions and divided into soluble and insoluble proteins as typically done for wheat gluten, carob germ proteins were found to be almost entirely ( approximately 95%) in the soluble fraction with only ( approximately 5%) in the insoluble fraction. As in wheat, SEC-MALS analysis showed that the insoluble proteins had a greater M(w) than the soluble proteins and ranged up to 8 x 10(7) Da. The lower M(w) distribution of the polymeric proteins of carob germ flour may account for differences in functionality between wheat and carob germ flour.

Gluten-free sorghum bread improved by sourdough fermentation: biochemical, rheological, and microstructural background.

This study was conducted to improve the quality and theoretical understanding of gluten-free sorghum bread. The addition of 2% hydroxypropyl methylcellulose improved bread based on 105% water, 70% sorghum flour, and 30% potato starch. Nevertheless, a flat top and tendency toward a hole in the crumb remained. Sourdough fermentation of the total sorghum flour eliminated these problems. Size-exclusion high-performance liquid chromatography demonstrated that during sourdough fermentation, proteins from the dough liquid were degraded to peptides smaller than kafirin monomers (<19 kDa). Laser scanning confocal microscopy showed aggregated protein in bread crumb without sourdough fermentation, whereas with sourdough fermentation, only small isolated patches of protein bodies embedded in matrix protein remained. In oscillatory temperature sweeps, sourdough fermentation caused a significantly higher resistance to deformation (|G*|) after gelatinization of the above batter relative to batters without sourdough. Results suggest that a strong starch gel, without interference of aggregated protein, is desirable for this type of bread.