PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR AMYLASE FROM A THERMOPHILIC STREPTOMYCETE

被引:17
作者
GOLDBERG, JD
EDWARDS, C
机构
[1] Department of Genetics and Microbiology, Liverpool, L69 3BX, Life Sciences Building
来源
JOURNAL OF APPLIED BACTERIOLOGY | 1990年 / 69卷 / 05期
关键词
D O I
10.1111/j.1365-2672.1990.tb01568.x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Goldberg, J.D. & Edwards, C. 1990. Purification and characterization of an extracellular amylase from a thermophilic streptomycete. Journal of Applied Bacteriology69, 712–717. A single extracellular alpha‐amylase (1,4‐α‐D‐glucan glucanohydrolase, EC 3.2.1.1) from Streptomyces thermoviolaceus subsp. apingens was purified to homogeneity by a starch adsorption method. SDS‐PAGE indicated that the enzyme had an apparent M, of 57 kDa and activity was optimal at a pH of 7–2 and a temperature of 55d̀C. It employed an endo‐active mechanism to liberate predominantly maltose, as well as smaller amounts of higher oligosaccharides when incubated with starch. EDTA inhibited enzyme activity, suggesting an involvement of a divalent cation in activity. The enzyme was also stabilized by divalent cations when heated and the results suggested a major role for Ca2+ ions for both activity and thermostability. The alpha‐amylase from S. thermoviolaceus displayed some similarities with commercially‐used streptomycete alpha‐amylases. Copyright © 1990, Wiley Blackwell. All rights reserved
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页码:712 / 717
页数:6
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