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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Applied microbiology and biotechnology 2015-01, Vol.99 (2), p.717-727
Hauptverfasser: Vester, Jan Kjølhede, Glaring, Mikkel Andreas, Stougaard, Peter
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
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.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-014-5931-0