exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment
A cold-active α-amylase, AmyI₃C₆, identified by a functional metagenomics approach was expressed in Escherichia coli and purified to homogeneity. Sequence analysis showed that the AmyI₃C₆amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapte...
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Veröffentlicht in: | Applied microbiology and biotechnology 2015-01, Vol.99 (2), p.717-727 |
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Sprache: | eng |
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Zusammenfassung: | A cold-active α-amylase, AmyI₃C₆, identified by a functional metagenomics approach was expressed in Escherichia coli and purified to homogeneity. Sequence analysis showed that the AmyI₃C₆amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapted enzymes, as did comparison of the kinetic parameters Kₘand kcₐₜto a mesophilic α-amylase. AmyI₃C₆was shown to be heat-labile. Temperature optimum was at 10–15 °C, and more than 70 % of the relative activity was retained at 1 °C. The pH optimum of AmyI₃C₆was at pH 8–9, and the enzyme displayed activity in two commercial detergents tested, suggesting that the AmyI₃C₆α-amylase may be useful as a detergent enzyme in environmentally friendly, low-temperature laundry processes. |
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ISSN: | 0175-7598 1432-0614 |
DOI: | 10.1007/s00253-014-5931-0 |