This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Labes, A.
Right arrow Articles by Schönheit, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Labes, A.
Right arrow Articles by Schönheit, P.
Agricola
Right arrow Articles by Labes, A.
Right arrow Articles by Schönheit, P.

 Previous Article  |  Next Article 

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.

Novel Members of Glycoside Hydrolase Family 13 Derived from Environmental DNA{triangledown}

Antje Labes,1,{dagger} Eva Nordberg Karlsson,2 Olafur H. Fridjonsson,3 Pernilla Turner,2,{ddagger} 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 {alpha}-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.


* Corresponding author. Mailing address: Institut für Allgemeine Mikrobiologie, Am Botanischen Garten 3-9, D-24118 Kiel, Germany. Phone: 49-431-8804328. Fax: 49-431-8802194. E-mail: peter.schoenheit{at}ifam.uni-kiel.de

{triangledown} Published ahead of print on 25 January 2008.

{dagger} Present address: Kieler Wirkstoffzentrum am IFM-GEOMAR, Am Kiel-Kanal 44, D-24106 Kiel, Germany.

{ddagger} Present address: Department of Chemical and Biological Engineering, University of Colorado at Boulder, 424 UCB, Boulder, CO 80309-0424.


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.