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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46525

Title: Purification and Characterization of the Amylase from a Small Abalone, Haliotis sieboldii.
Authors: Meng-Shun Hsieh
Li-Jung Yin
Shann-Tzong Jiang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: purification of amylase
amylase sequence
characteristics of amylase
Date: 2008
Issue Date: 2018-05-22T07:20:08Z
Publisher: Fisheries Science
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.
Relation: 74(2) pp.425–432
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46525
Appears in Collections:[食品科學系] 期刊論文

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