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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38419

Title: Purification and properties of an extracellular α-amylase from Thermus sp. Bot. Bull.
Authors: Jei-Fu Shaw
Fu-Pang Lin
Su-Chiu Chen
Hsing-Chen Chen
Contributors: 國立臺灣海洋大學:生命科學暨生物科技學系
Keywords: Thermus sp.
Purified
Thermostable extracellular a-amylase
Date: 1995
Issue Date: 2016-09-01T03:06:17Z
Abstract: Abstract: An extracellular a-amylase from an extreme thermophile, Thermus sp., was highly purified by affinity absorption on starch granules. SDS-PAGE showed a single band for the purified enzyme, with an apparent molecular weight of 59000. The optimum pH and temperature for the enzyme action on starch was 5.5_6.5 and 70°C, respectively. The enzyme randomly attacked the bonds in the inner region of the starch and produced various maltooligosaccharides. The minimum length of maltooligosaccharide cleaved by this enzyme was maltohexaose. The enzyme activity was strongly inhibited by the addition of Cu2+ and Fe2+ ions. The enzyme belonged to the EDTA-sensitive a-amylase group, but its activity was not stimulated by the presence of Ca2+ ions.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38419
Appears in Collections:[生命科學系] 期刊論文

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