ArticleMolecular biotechnology2016
Cloning, Expression, and Characterization of a Novel L-Arabinose Isomerase from the Psychrotolerant Bacterium Pseudoalteromonas haloplanktis.
Article in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 17 citations in OpenAlex.
- Discovery and Preliminary Characterization of Lactose-Transforming Enzymes inInternational journal of molecular sciences · 2026Article
- Development and Characterization of a Tunable Metal-Organic Framework (MOF) for the Synthesis of a Rare Sugar D-Tagatose.Applied biochemistry and biotechnology · 2025Article
- Alternative Heterologous Expression of L-Arabinose Isomerase from Enterococcus faecium DBFIQ E36 By Residual Whey Lactose Induction.Molecular biotechnology · 2021Article
- Exploring a Highly D-Galactose Specific L-Arabinose Isomerase FromFrontiers in bioengineering and biotechnology · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-Arabinose isomerase (L-AI, EC 5.3.1.4) catalyzes the isomerization between L-arabinose and L-ribulose, and most of the reported ones can also catalyze D-galactose to D-tagatose, except Bacillus subtilis L-AI. In this article, the L-AI from the psychrotolerant bacterium Pseudoalteromonas haloplanktis ATCC 14393 was characterized. The enzyme showed no substrate specificity toward D-galactose, which was similar to B. subtilis L-AI but distinguished from other reported L-AIs. The araA gene encoding the P. haloplanktis L-AI was cloned and overexpressed in E. coli BL21 (DE3). The recombinant enzyme was purified by one-step nickel affinity chromatography . The enzyme displayed the maximal activity at 40 °C and pH 8.0, and showed more than 75 % of maximal activity from pH 7.5-9.0. Metal ion Mn
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