ArticleExtremophiles : life under extreme conditions2012
Cyclodextrin glycosyltransferase: a key enzyme in the assimilation of starch by the halophilic archaeon Haloferax mediterranei.
Article in Extremophiles : life under extreme conditions, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- An Archaeal Cyclodextrin Glycosyltransferase fromInternational journal of molecular sciences · 2026Article
- Pharmaceutical applications of halophilic enzymes.Heliyon · 2025Review
- Production of Poly(3-hydroxybutyrate-Bioengineering (Basel, Switzerland) · 2024Article
- Characterization of an Amylolytic Enzyme from Massilia timonae of the GH13_19 Subfamily with Mixed Maltogenic and CGTase Activity.Applied biochemistry and biotechnology · 2023Article
- Molecular cloning, and optimized production and characterization of recombinant cyclodextrin glucanotransferase from3 Biotech · 2022Article
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
- Halophilic archaea and their potential to generate renewable fuels and chemicals.Biotechnology and bioengineering · 2021Review
- Review
- Genome-Wide Association Study on Total Starch, Amylose and Amylopectin in Barley Grain Reveals Novel Putative Alleles.International journal of molecular sciences · 2021Article
- Biotechnological applications of archaeal enzymes from extreme environments.Biological research · 2018Review
- Improved activity of β-cyclodextrin glycosyltransferase from Bacillus sp. N-227 via mutagenesis of the conserved residues.3 Biotech · 2017Article
- A novel cyclodextrin glucanotransferase from an alkaliphile Microbacterium terrae KNR 9: purification and properties.3 Biotech · 2016Article
- Halophiles: biology, adaptation, and their role in decontamination of hypersaline environments.World journal of microbiology & biotechnology · 2016Review
- Recombinant cyclodextrinase from Thermococcus kodakarensis KOD1: expression, purification, and enzymatic characterization.Archaea (Vancouver, B.C.) · 2015Article
- Thermophilic and halophilic β-agarase from a halophilic archaeon Halococcus sp. 197A.Extremophiles : life under extreme conditions · 2013Article
- Diversity and subcellular distribution of archaeal secreted proteins.Frontiers in microbiology · 2012Article
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6 authors.
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Abstract
A cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) was successfully isolated and characterized from the halophilic archaeon Haloferax mediterranei. The enzyme is a monomer with a molecular mass of 77 kDa and optimum activity at 55°C, pH 7.5 and 1.5 M NaCl. The enzyme displayed many activities related to the degradation and transformation of starch. Cyclization was found to be the predominant activity, yielding a mixture of cyclodextrins, mainly α-CD, followed by hydrolysis and to a lesser extent coupling and disproportionation activities. Gene encoding H. mediterranei CGTase was cloned and heterologously overexpressed. Sequence analysis revealed an open reading frame of 2142 bp that encodes a protein of 713 amino acids. The amino acid sequence displayed high homology with those belonging to the α-amylase family. The CGTase is secreted to the extracellular medium by the Tat pathway. Upstream of the CGTase gene, four maltose ABC transporter genes have been sequenced (malE, malF, malG, malK). The expression of the CGTase gene yielded a fully active CGTase with similar kinetic behavior to the wild-type enzyme. The H. mediterranei CGTase is the first halophilic archaeal CGTase characterized, sequenced and expressed.
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