Among cereal proteins, rice proteins are hypoallergenic, rich in essential amino acids and easily digestible etc. While their lower solubilities under neutral conditions limit their applications in food industry. In present study, the physicochemical and structural properties of rice glutelin at different pH values (pH 3.0, 4.0 and 7.0) were characterized to explore the optimum pH value to dissolve rice protein and expand its application range. The results showed that, compared to the neutral condition, the solubility and structural properties of rice glutelin were changed significantly under the acidic conditions. The protein solubility was only (6.24±1.25)% at pH 7.0, for under neutral condition, protein molecules linked together to form huge molecular aggregates. However, under acidic conditions, protein molecules dissociated and intermolecular disulfide bonds ruptured gradually. Therefore, the protein solubility increased under the acidic condition, and it reached (72.47±2.36)% at pH 3.0.