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  4. A highly thermoactive and salt-tolerant α-amylase isolated from a pilot-plant biogas reactor
 
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A highly thermoactive and salt-tolerant α-amylase isolated from a pilot-plant biogas reactor

Publikationstyp
Journal Article
Date Issued
2013
Sprache
English
Author(s)
Jabbour, Dinar  
Sorger, Anneke  
Sahm, Kerstin  
Antranikian, Garabed  
Institut
Technische Mikrobiologie V-7  
TORE-URI
http://hdl.handle.net/11420/3301
Journal
Applied microbiology and biotechnology  
Volume
97
Issue
7
Start Page
2971
End Page
2978
Citation
Applied Microbiology and Biotechnology 7 (97): 2971-2978 (2013)
Publisher DOI
10.1007/s00253-012-4194-x
Scopus ID
2-s2.0-84876681193
Publisher
Springer
Aiming at the isolation of novel enzymes from previously uncultured thermophilic microorganisms, a metagenome library was constructed from DNA isolated from a pilot-plant biogas reactor operating at 55 °C. The library was screened for starch-degrading enzymes, and one active clone was found. An open reading frame of 1,461 bp encoding an α-amylase from an uncultured organism was identified. The amy13A gene was cloned in Escherichia coli, resulting in high-level expression of the recombinant amylase. The novel enzyme Amy13A showed the highest sequence identity (75 %) to α-amylases from Petrotoga mobilis and Halothermothrix orenii. Amy13A is highly thermoactive, exhibiting optimal activity at 80 °C, and it is also highly salt-tolerant, being active in 25 % (w/v) NaCl. Amy13A is one of the few enzymes that tolerate high concentrations of salt and elevated temperatures, making it a potential candidate for starch processing under extreme conditions. © 2012 The Author(s).
Subjects
α-Amylase
Calcium-dependent
Glycoside hydrolase family 13
Halophile
Metagenome
Petrotoga
Thermophile
DDC Class
500: Naturwissenschaften
570: Biowissenschaften, Biologie
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