An α-galactosidase designated as TAG was purified from the dried fruit bodies of Tremella aurantialba with 182.5-fold purification. The purification procedure involved ion exchange chromatography on Q-sepharose, DEAE-Cellulose, and Mono Q and gel filtration by FPLC on Superdex 75. The purified α-galactosidase was a monomeric protein with a molecular mass of 88 kDa. The optimal pH of TAG was 5.0 and more than 60% of the original enzyme activity remained at pH 2.0 and 3.0. Its optimal temperature was 54 °C with good thermo-stability, 30.8% of the original activity was retained after exposure to a temperature of 70 °C for 1 h. The metal ions Hg2+, Cu2+, Fe3+ and Mg2+ strongly inhibited the enzyme activity. The enzyme activity was found to be inhibited by N-bromosuccinimide indicating that tryptophan was essential to the catalytic activity of α-galactosidase. The enzyme completely hydrolysed stachyose and partially hydrolysed raffinose to galactose at 50 °C within 6 h as detected by thin layer chromatography and the dinitrosalicylic acid method and the content of reducing sugar reached 4.36 mg/mL.