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Identification of a halophilic α-amylase gene from Escherichia coli JM109 and characterization of the recombinant enzyme.
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- Author(s): Wei Y;Wei Y; Wang X; Liang J; Li X; Du L; Huang R
- Source:
Biotechnology letters [Biotechnol Lett] 2013 Jul; Vol. 35 (7), pp. 1061-5. Date of Electronic Publication: 2013 Mar 12.
- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Kluwer Academic Publishers Country of Publication: Netherlands NLM ID: 8008051 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1573-6776 (Electronic) Linking ISSN: 01415492 NLM ISO Abbreviation: Biotechnol Lett Subsets: MEDLINE
- Publication Information:
Publication: 1999- : Dordrecht : Kluwer Academic Publishers
Original Publication: [Kew, Eng., Science and Technology Letters]
- Subject Terms:
- Abstract:
A halophilic α-amylase (EAMY) gene from Escherichia coli JM109 was overexpressed in E. coli XL10-Gold and the recombinant protein was purified and characterized. The activity of the EAMY depended on the presence of both Na(+) and Cl(-), and had maximum activity in 2 M NaCl at 55 °C and pH 7.0. When 2% (w/v) soluble starch was used as substrate, the specific activity was about 1,090 U mg(-1) protein. This is the first report on identifying a halophilic α-amylase with high specific activity from non-halophilic bacteria.
- Accession Number:
0 (Coenzymes)
0 (Recombinant Proteins)
4R7X1O2820 (Chlorine)
9005-25-8 (Starch)
9NEZ333N27 (Sodium)
EC 3.2.1.1 (alpha-Amylases)
- Publication Date:
Date Created: 20130313 Date Completed: 20131213 Latest Revision: 20130611
- Publication Date:
20231215
- Accession Number:
10.1007/s10529-013-1175-9
- Accession Number:
23479413
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