Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Novel members of glycoside hydrolase family 13 derived from environmental DNA

Labes, Antje ; Nordberg Karlsson, Eva LU orcid ; Fridjonsson, Olafur H ; Turner, Pernilla LU ; Hreggvidson, Gudmundur O ; Kristjansson, Jakob K ; Holst, Olle LU and Schönheit, Peter (2008) In Applied and Environmental Microbiology 74(6). p.1914-1921
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Applied and Environmental Microbiology
volume
74
issue
6
pages
1914 - 1921
publisher
American Society for Microbiology
external identifiers
  • wos:000254065600029
  • scopus:40849140824
  • pmid:18223106
  • pmid:18223106
ISSN
0099-2240
DOI
10.1128/AEM.02102-07
language
English
LU publication?
yes
additional info
Published online ahead of print on 25 January 2008
id
59f9f6fe-fd0a-485f-a4ce-3dbfcd56d5b5 (old id 1191663)
date added to LUP
2016-04-01 11:52:14
date last changed
2022-01-26 19:26:08
@article{59f9f6fe-fd0a-485f-a4ce-3dbfcd56d5b5,
  abstract     = {{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.}},
  author       = {{Labes, Antje and Nordberg Karlsson, Eva and Fridjonsson, Olafur H and Turner, Pernilla and Hreggvidson, Gudmundur O and Kristjansson, Jakob K and Holst, Olle and Schönheit, Peter}},
  issn         = {{0099-2240}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{1914--1921}},
  publisher    = {{American Society for Microbiology}},
  series       = {{Applied and Environmental Microbiology}},
  title        = {{Novel members of glycoside hydrolase family 13 derived from environmental DNA}},
  url          = {{http://dx.doi.org/10.1128/AEM.02102-07}},
  doi          = {{10.1128/AEM.02102-07}},
  volume       = {{74}},
  year         = {{2008}},
}