Novel members of glycoside hydrolase family 13 derived from environmental DNA.

Labes, Antje, Nordberg Karlsson, E., Fridjonsson, O. H., Turner, P., Hreggvidson, G. O., Kristjansson, J. K., Holst, Olle and Schönheit, Peter (2008) Novel members of glycoside hydrolase family 13 derived from environmental DNA. Applied and Environmental Microbiology, 74 (6). pp. 1914-1921. DOI 10.1128/AEM.02102-07.

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Starch and pullulan-modifying enzymes of the α-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.

Document Type: Article
Research affiliation: OceanRep > GEOMAR > FB3 Marine Ecology > FB3-MI Marine Microbiology
Refereed: Yes
Open Access Journal?: No
DOI etc.: 10.1128/AEM.02102-07
ISSN: 0099-2240
Date Deposited: 03 Dec 2008 16:52
Last Modified: 26 Apr 2016 11:42

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