期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 72, 期 -, 页码 290-298出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2014.08.023
关键词
alpha-Amylase; Bacillus subtilis DR8806; Cloning; Organic solvent; Maltotriose, Thermotolerant
资金
- Institute of Biotechnology and research council of Ferdowsi University of Mashhad - Iran [3/27142, 23-2-1392, 4065, 06-02-1389]
The gene encoding an extracellular alpha-amylase from Bacillus subtilis DR8806 was cloned into pET28a(+) vector and expressed in Escherichia coli BL21 (DE3). The recombinant enzyme with molecular mass of 76 kDa exhibited optimal activity at pH 5.0 and 70 degrees C with high stability in pH and temperature ranges of 4.0-9.0 and 45-75 degrees C. The enzyme showed a half-life of 125 min at 70 degrees C. The alpha-amylase activity enhanced in the presence of Na+, K+, and Ca2+ ions, while Zn2+, Pb2+, and Hg2+ ions inhibited the activity. The recombinant alpha-amylase exhibited high stability towards ioninc detergents sodium dodecyl sulfate (SDS) and cetyl trimethylammonium bromide (CTAB). Organic solvents in reaction media increased the or-amylase activity. TLC analysis showed that maltoriose and maltose were the major end products of enzymatic starch hydrolysis. Presenting various properties of recombinant or-amylase makes it well suited as a potential candidate for industrial usages. (C) 2014 Elsevier B.V. All rights reserved.
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