Abstract: After salting out with ammonium sulfate, chromatography with DEAE-Sepharose and Sephacryl S-200, SOD was purified from royal jelly of the Italian worker bee, Apis mellifera with purification factor of 104.00, and the specific activity 53.05 U/mg proteins. The obtained enzyme showed a single band on SDSPAGE. The effect of temperature on SOD activity was studied, and it was found that the enzyme was very stable. The contents of Cu, Zn, Fe, and Mn was also studied, and it was found that the enzyme contained Cu and Zn. Circular dichroism spectrum was investigated and it was found that the proportion of α-helix,β-sheet and random coiling form of proteins was 26.1%,53.8% and 22.0% respectively. The isoelectric focusing of SOD indicated that pI of the enzyme contained intrachain disulfate bond. The amino acid composition was investigated and it was found that the enzyme contained 402 amino acid residues. The enzyme had relatively high content of Asp, Gly, Leu, Ala, Glu and Val. Both urea and BrAc could inhibit enzyme activity, lead the change of ultraviolet absorption and induce the decrease of fluorescence emission. DTT could lead the change of enzyme activity, the increase of ultraviolet absorption and the decrease of fluorescence emission.

Key words: Apis mellifera, royal jelly, SOD, isolation, purification, biochemical properties