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Applied and Environmental Microbiology, March 2008, p. 1914-1921, Vol. 74, No. 6
0099-2240/08/$08.00+0 doi:10.1128/AEM.02102-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Eva Nordberg Karlsson,2
Olafur H. Fridjonsson,3
Pernilla Turner,2,
Gudmundur O. Hreggvidson,3
Jakob K. Kristjansson,3
Olle Holst,2 and
Peter Schönheit1*
Institut für Allgemeine Mikrobiologie, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, DE-24118 Kiel, Germany,1 Department of Biotechnology, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden,2 Prokaria Ltd., Gylfaflöt 5, IS-112 Reykjavik, Iceland3
Received 13 September 2007/ Accepted 12 January 2008
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 that correlated with enzymatic activities were identified; e.g., the presence of the N domain was correlated with cyclodextrinase activity. The enzymes exhibited stability under thermophilic conditions and showed features appropriate for biotechnological applications.
Published ahead of print on 25 January 2008.
Present address: Kieler Wirkstoffzentrum am IFM-GEOMAR, Am Kiel-Kanal 44, D-24106 Kiel, Germany.
Present address: Department of Chemical and Biological Engineering, University of Colorado at Boulder, 424 UCB, Boulder, CO 80309-0424.
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