Purification and characterization of the amylase from a small abalone Haliotis sieboldii |
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Authors: | Meng-Shun Hsieh Li-Jung Yin Shann-Tzong Jiang |
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Affiliation: | National Taiwan Ocean University, Keelung 202,;Department of Sea Food Science, National Kaohsiung Marine University, Kaohsiung, and;Department of Food and Nutrition, Providence University, Shalu, Taichung County 43301, Taiwan |
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Abstract: | ABSTRACT: 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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Keywords: | abalone amylase sequence amylase characteristics of amylase purification of amylase |
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