The mechanism of alkali-induced rice protein gel formation: Effect of alkali concentration and temperature

Abstract

Rice protein (RP) is a high-quality hypoallergenic plant protein, but its extremely poor water solubility makes it difficult to be applied in liquid food systems. Therefore, in-depth exploration of its gel properties is an effective way to broaden the application scenarios of RP. In this work, it was first found that the rate and strength of gel formation by RP at 25 °C strongly depended on the increase in alkali concentration (from 0.05 M to 0.125 M), i.e., alkali concentrations above 0.075 M were sufficient to induce the formation of a stable gel by 10% (w/v) of RP in 0.5 h. Increasing the temperature during alkali-induced RP gel formation (50 °C, 80 °C) greatly increased the rate of gel formation, whereas prolonged (>30 min) heat treatment resulted in liquefaction of the gel. A more in-depth analysis revealed that the alkali was able to depolymerize glutelin within the agglomerates in its native state, thereby forming a gel network among glutelin molecules at lower alkali concentrations (CNaOH = 0.075 M) mainly through hydrophobic interactions. Whereas, higher alkali concentration (CNaOH = 0.125 M) resulted in the rapid transformation of exposed free sulfhydryl groups into disulfide bonds, thus exerting a major contribution to the gel network, followed by hydrogen bonding. Furthermore, the phenomenon of heat-induced gel liquefaction was mainly attributed to the dissociation of glutelin subunits and was accompanied by an increase in the disordered structure of proteins in the amide III region. These findings may provide a scientific basis for the development of rice protein gel foods.