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- W2019295502 abstract "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." @default.
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- W2019295502 date "2012-06-29" @default.
- W2019295502 modified "2023-09-23" @default.
- W2019295502 title "A highly thermoactive and salt-tolerant α-amylase isolated from a pilot-plant biogas reactor" @default.
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- W2019295502 doi "https://doi.org/10.1007/s00253-012-4194-x" @default.
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