Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice

Rice proteins, as a cheap plant protein source from the by-products of rice dreg processing, could potentially replace commonly used proteins such as soy and whey proteins in selected food products. In this study, the functional properties, surface hydrophobicity (H0), sulfhydryl and disulfide bond contents, thermal properties, as well as secondary structures of native rice endosperm protein (REP) and processed rice dreg protein (RDP) extracted from long-grain indica rice, were compared. RDP was found to have a higher solubility associated with its relatively higher emulsifying and foaming properties than REP, as well as its water/oil holding capacity, although it was a denatured protein. The emulsifying properties were dependent on the solubility and H0, while solubility was also related to the disulfide bond contents. Distinct differences in H0, thermal properties, and disulfide bond contents between REP and RDP could be due to the conformational changes, as the industrial processing steps in the production of rice syrups caused an increase in β-turns at the expense of β-sheets and random coils of REP, leading to the unfolding of β-sheets into higher-ordered supramolecular structures for RDP, which could be responsible for its better functional properties.

► Rice dreg protein (RDP) is a low cost, denatured protein source from rice endosperm protein (REP), with >50% protein content.
► The processed RDP had better functional properties than Native REP.
► The industrial processing steps caused conformational changes of REP.
► RDP had formed higher-ordered supramolecular structures.