ArticleApplied and environmental microbiology2004
Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima.
Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 137 citations in OpenAlex.
- Advances in the Production of D-Tagatose Using L-Arabinose Isomerase.Microorganisms · 2026Review
- Abilities of Rare Sugar Members to Release Glucagon-like Peptide-1 and Suppress Food Intake in Mice.Nutrients · 2025Article
- Transforming monosaccharides: Recent advances in rare sugar production and future exploration.BBA advances · 2025Article
- Preparation of combined cross-linked enzyme aggregates containing galactitol dehydrogenase and NADH oxidase for L-tagatose synthesis via in situ cofactor regeneration.Bioprocess and biosystems engineering · 2022Article
- Trends in lactose-derived bioactives: synthesis and purification.Systems microbiology and biomanufacturing · 2022Review
- Construction and Validation of a Genome-Scale Metabolic Network of Thermotoga sp. Strain RQ7.Applied biochemistry and biotechnology · 2021Article
- Exploring a Highly D-Galactose Specific L-Arabinose Isomerase FromFrontiers in bioengineering and biotechnology · 2020Article
- Biochemical Characterization of Heat-Tolerant Recombinant L-Arabinose Isomerase from Enterococcus faecium DBFIQ E36 Strain with Feasible Applications in D-Tagatose Production.Molecular biotechnology · 2019Article
- Biochemical properties of L-arabinose isomerase from Clostridium hylemonae to produce D-tagatose as a functional sweetener.PloS one · 2018Article
- Engineering the l-Arabinose Isomerase from Enterococcus Faecium for d-Tagatose Synthesis.Molecules (Basel, Switzerland) · 2017Article
- TM0416, a Hyperthermophilic Promiscuous Nonphosphorylated Sugar Isomerase, Catalyzes Various CApplied and environmental microbiology · 2017Article
- Cloning, Expression, and Characterization of a Novel L-Arabinose Isomerase from the Psychrotolerant Bacterium Pseudoalteromonas haloplanktis.Molecular biotechnology · 2016Article
- Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production.BMC biotechnology · 2016Article
- The secreted L-arabinose isomerase displays anti-hyperglycemic effects in mice.Microbial cell factories · 2015Article
- Facile Enzymatic Synthesis of Ketoses.Angewandte Chemie (International ed. in English) · 2015Article
- Protein purification, crystallization and preliminary X-ray diffraction analysis of L-arabinose isomerase from Lactobacillus fermentum CGMCC2921.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Crystallization and preliminary X-ray crystallographic analysis of L-arabinose isomerase from thermophilic Geobacillus kaustophilus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Homologous Alkalophilic and Acidophilic L-Arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability.Applied and environmental microbiology · 2012Article
- A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c.Microbial cell factories · 2012Article
- Heterologous expression and characterization of Bacillus coagulans L-arabinose isomerase.World journal of microbiology & biotechnology · 2012Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The araA gene encoding L-arabinose isomerase (AI) from the hyperthermophilic bacterium Thermotoga maritima was cloned and overexpressed in Escherichia coli as a fusion protein containing a C-terminal hexahistidine sequence. This gene encodes a 497-amino-acid protein with a calculated molecular weight of 56,658. The recombinant enzyme was purified to homogeneity by heat precipitation followed by Ni(2+) affinity chromatography. The native enzyme was estimated by gel filtration chromatography to be a homotetramer with a molecular mass of 232 kDa. The purified recombinant enzyme had an isoelectric point of 5.7 and exhibited maximal activity at 90 degrees C and pH 7.5 under the assay conditions used. Its apparent K(m) values for L-arabinose and D-galactose were 31 and 60 mM, respectively; the apparent V(max) values (at 90 degrees C) were 41.3 U/mg (L-arabinose) and 8.9 U/mg (D-galactose), and the catalytic efficiencies (k(cat)/K(m)) of the enzyme were 74.8 mM(-1).min(-1) (L-arabinose) and 8.5 mM(-1).min(-1) (D-galactose). Although the T. maritima AI exhibited high levels of amino acid sequence similarity (>70%) to other heat-labile mesophilic AIs, it had greater thermostability and higher catalytic efficiency than its mesophilic counterparts at elevated temperatures. In addition, it was more thermostable in the presence of Mn(2+) and/or Co(2+) than in the absence of these ions. The enzyme carried out the isomerization of D-galactose to D-tagatose with a conversion yield of 56% for 6 h at 80 degrees C.
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