|Tilley, Michael - Mike|
|Park, Seok Ho|
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 9/15/2008
Publication Date: 9/21/2008
Citation: Smith, B.M., Schober, T.J., Bean, S., Tilley, M., Park, S., Aramouni, F.H., Herald, T.J. 2008. Characterization of the functional properties of carob germ proteins. Meeting Abstract. Cereal Foods World. 53:A79.
Technical Abstract: Proteins from the carob germ were identified as having gluten-like proteins in 1935. While some biochemical characterization of carob germ proteins and their functionality has been carried out, relatively little has been done when compared to proteins such as gluten. Carob germ proteins were separated into soluble proteins and insoluble proteins using an SDS phosphate buffer without a reducing agent. The SDS soluble proteins (SP) constituted almost 96% of the proteins and the insoluble proteins (IP) only 4%. Of the SP, roughly 65% were polymers or small oligomers with the remaining 35% monomeric proteins. IP were essentially all large polymeric proteins. Reduction of the SP and IP after extraction revealed that the majority of the polymeric proteins were disulfide-linked. Mixing in a farinograph in the presence of different solvents was done to determine which types of bonds are important in carob dough formation. DTT was found to destroy the mixing curve, demonstrating the importance of disulfide bonds during carob mixing. Bread baked from carob dough had loaf volume and crumb structure similar to those of wheat breads, and a specific volume of ~3mL/g.