Purification and characterization of the amylase from a small abalone Haliotis sieboldii

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 Ba2+, Mg2+, Ca2+, Co2+, Ni2+, Mn2+, K+, Ag+, Na+ and Li+, but completely or partially inhibited by Al3+, Cu2+, Cd2+, Hg2+ and Zn2+. 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 α-amylase.

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