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The effect of heat treatment on solubility, surface hydrophobicity and structure of rice bran albumin and globulin were characterised. The differential scanning calorimetry (DSC), FT-IR and Raman spectra were used to analyse the effect. The results of DSC analysis showed that albumin denatured after a thermal pre-treatment of 70 °C, while globulin denatured at 90 °C. The solubility of albumin sharply decreased after heat treatment, while the solubility of globulin decreased by up to 100 °C. The results of FT-IR demonstrated that heating globulin generally increased the content of α-helix and β-turn structure, but reduced β-sheet and random coil structures, while heating albumin produced a pronounced increase in α-helix and β-sheet structures from random coil and β-turn structures. Heating albumin decreased regions around 33 kDa but increased relative band intensity around 45-53 kDa in SDS-PAGE pattern, while heating globulin up to 90 °C caused losses in bands around 20 and 50 kDa. Raman spectrogram showed that heating albumin induced a slight decrease in intensity of the Trp band. However, the Trp band of heated globulin did not change.