AEM Accepts, published online ahead of print on 25 January 2008

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Appl. Environ. Microbiol. doi:10.1128/AEM.02102-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Isolation of new members of glycoside hydrolase family 13 derived from environmental DNA

Antje Labes, Eva Nordberg Karlsson, Olafur H. Fridjonsson, Pernilla Turner, Gudmundur O. Hreggvidson, Jakob K. Kristjansson, Olle Holst, and Peter Schönheit^*

Institut für Allgemeine Mikrobiologie, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, DE-24118 Kiel, Germany; Department of Biotechnology, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden; Prokaria Ltd, Gylfaflöt 5, IS-112 Reykjavik, Iceland

^* To whom correspondence should be addressed. Email: peter.schoenheit{at}ifam.uni-kiel.de.

Starch and pullulan-modifying enzymes of the -amylase family (glycoside hydrolase family 13) have several industrial applications. To date, most of these enzymes have been derived from isolated organisms. To increase the number of members of this enzyme family, in particular of the thermophilic representatives, we have applied a consensus-primer-based approach using DNA from enrichments from geothermal habitats. With this approach we succeeded in isolating three new enzymes: a neopullulanase and two cyclodextrinases. Both cyclodextrinases displayed significant maltogenic amylase side-activity, while one showed significant neopullulanase side-activity. Specific motifs and domains could be identified, which correlated with their enzymatic activities; e.g. the presence of domain was correlated to cyclodextrinase activity. The enzymes exhibited stability at thermophilic conditions, which showed features appropriate for biotechnological applications.