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   <subfield code="a">An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment</subfield>
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   <subfield code="c">[Jan Vester, Mikkel Glaring, Peter Stougaard]</subfield>
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   <subfield code="a">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 pH8-9, 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.</subfield>
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