Abstract
Dispersion of rice protein (RP) at a neutral pH is highly important for its application in the food industry. We analyzed the solubility of RP at different pH conditions and found higher solubility at pH < 3 and pH > 8 than at a neutral pH. Furthermore, at pH 2, the RP solubility improved from 30 to 63% with sonication; however, the samples precipitated when the pH was increased from 2 to 7. To circumvent this, anionic pectin and sodium alginate were added to the RP solution at pH 2. Pectin formed a complex with RP at pH 2, showing a shift in the zeta-potential from 17.3mV (RP only) to - 1.0mV (RP plus 1% pectin). Interestingly, the formation of this RP-pectin complex allowed RP to remain dispersed when the pH was increased to 7. Moreover, a stable emulsion could be prepared using the RP-pectin complex as an emulsifier.
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