An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment
Research output: Contribution to journal › Journal article › Research › peer-review
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 AmyI3C6 amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapted enzymes, as did comparison of the kinetic parameters Km and kcat to a mesophilic α-amylase. AmyI3C6 was 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 AmyI3C6 was at pH 8-9, and the enzyme displayed activity in two commercial detergents tested, suggesting that the AmyI3C6 α-amylase may be useful as a detergent enzyme in environmentally friendly, low-temperature laundry processes.
Original language | English |
---|---|
Journal | Applied Microbiology and Biotechnology |
Volume | 99 |
Issue number | 2 |
Pages (from-to) | 717-727 |
Number of pages | 11 |
ISSN | 0175-7598 |
DOIs | |
Publication status | Published - 2015 |
- α-Amylase, Alkaline-active, Clostridia, Cold-active, Detergents, Heat-labile
Research areas
ID: 130476116