| Literature DB >> 25038927 |
Jan Kjølhede Vester1, Mikkel Andreas Glaring, Peter Stougaard.
Abstract
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 K m and k cat 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.Entities:
Mesh:
Substances:
Year: 2014 PMID: 25038927 DOI: 10.1007/s00253-014-5931-0
Source DB: PubMed Journal: Appl Microbiol Biotechnol ISSN: 0175-7598 Impact factor: 4.813