TITLE	Purification and properties of an extracellular a-amylase from Thermus sp.
AUTHOR	Jei-Fu Shaw Institute of Marine Biotechnology, National Taiwan Ocean University, Keelung, Taiwan 202, Republic of China Fu-Pang Lin Institute of Marine Biotechnology, National Taiwan Ocean University, Keelung, Taiwan 202, Republic of China Su-Chiu Chen Institute of Botany, Academia Sinica, Taipei, Taiwan 115, Republic of China Hsing-Chen Chen Department of Marine Food Science, National Taiwan Ocean University, Keelung, Taiwan 202, Republic of China
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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.
KEYWORD	Purified; Thermostable extracellular a-amylase; Thermus sp;
ARTICLE INFO	Botanical Bulletin of Academia Sinica, Volume 36 Number 3 July 1995, page 195-200, 6 pages
PUBLISHER	Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan, Republic of China