Rice protein isolates, glutelin, Langi, Functional properties (May 2005)
Agboola, S Ng, D Mills, D
This study focused on the technique of isolating albumin, globulin, glutelin and prolamin fractions in the Australian rice variety Langi. The technique of capilllary elcectrophoresis (SDS-CE) and Sodium dodecyl sulphate polyacrylmaide gel electrophories (SDS-PAGE) was used to characterize yield, protein content and molecular weight profile. In conjunction with this the heating of starch to 700C and influence of pre extraction enzymatic hydrolysis and the single extraction of glutelin fraction was also examined. The study concluded that the method, particularly the pre extraction processing, used for isolating rice protein fractions, affects their purity and protein profile by CE. It seems however that these differences do not affect functional properties of the main protein (glutelin) fraction which possesses good gelling properties. It was suggested that additional studies aimed at improving solubility, emulsifying and foaming properties of the glutelin fraction should focus on enzymatic hydrolysis and the reduction of disulphide bonds.