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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46535

Title: Purification and Characterization of Amylases from Small Abalone (Sulculus diversicolor aquatilis)
Authors: Ching-Yu Tsao
Yun-Zu Pan
Shann-Tzong Jiang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: abalone
Amylase
characteristics of amylase
purification of amylase
Date: 2003
Issue Date: 2018-05-23T01:15:09Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract: Amylases II-1 and II-2 with molecular weights of 55.7 and 65 kDa, respectively, were purified to electrophoretical homogeneity from small abalone (Sulculus diversicolor aquatilis) by ammonium sulfate fractionation, Sepharose CL-6B, CM-Sepharose CL-6B, and Sephacryl S-100 chromatographs. They had optimal temperatures of 45 and 50 °C and an optimal pH of 6.0. The purified amylases were stable at pH 5.0−8.0 and 6.0−8.0, respectively. They were completely or partially inhibited by Hg2+, Cu2+, Cd2+, Zn2+, iodoacetamide, phenylmethanesulfonyl fluoride, and N-ethylmaleimide, suggesting the existence of cysteine at their active sites. Digestion tests against various polysaccharides suggested that the purified amylases II-1 and II-2 are neoamylases which can hydrolyze both α-1,4 and α-1,6 glucosidic bonds. Amylase II-2 might be an exo- and II-1 an endo-/exo-amylase.
Relation: 51(4) pp.1064–1070
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46535
Appears in Collections:[食品科學系] 期刊論文

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