Amylase, with MW of 59 kDa, was purified from small abalone Haliotis sieboldii by ammonium sulfate fractionation, CM Sepharose Fast Flow and Sephacryl S-100 HR chromatographies. The optimal pH and temperature of purified amylase were 6.0 and 37°C, respectively. The purified enzyme was stable at pH 6.0-8.0 and low temperatures. It was activated by Ba 2+ , Mg 2+ , Ca 2+ , Co 2+ , Ni 2+ , Mn 2+ , K + , Ag + , Na + and Li + , but completely or partially inhibited by Al 3+ , Cu 2+ , Cd 2+ , Hg 2+ and Zn 2+ . EDTA could completely inhibit, while iodoacetamide, N-ethylmaleimide and urea partially inhibit the purified amylase. According to the digestion mode of various polysaccharides, the purified enzyme was considered to be an a-amylase.KEY WORDS: abalone, amylase sequence, amylase, characteristics of amylase, purification of amylase.