ArticleApplied and environmental microbiology2008
Novel members of glycoside hydrolase family 13 derived from environmental DNA.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 34 citations in OpenAlex.
- Mining thermophiles for biotechnologically relevant enzymes: evaluating the potential of European and Caucasian hot springs.Extremophiles : life under extreme conditions · 2023Review
- Discovery of a New Microbial Origin Cold-Active Neopullulanase Capable for Effective Conversion of Pullulan to Panose.International journal of molecular sciences · 2022Article
- Article
- Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach.Extremophiles : life under extreme conditions · 2019Article
- Improved soluble expression of the gene encoding amylolytic enzyme Amo45 by fusion with the mobile-loop-region of co-chaperonin GroES inBiocatalysis and biotransformation · 2013Article
- Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues.The protein journal · 2011Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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