ArticleWorld journal of microbiology & biotechnology2012
Heterologous expression and characterization of Bacillus coagulans L-arabinose isomerase.
Article in World journal of microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Advances in the Production of D-Tagatose Using L-Arabinose Isomerase.Microorganisms · 2026Review
- Engineering the L-Arabinose Isomerase fromMolecules (Basel, Switzerland) · 2026Article
- Recent advances in properties, production, and applications of L-ribulose.Applied microbiology and biotechnology · 2020Review
- Characterization of a D-lyxose isomerase from Bacillus velezensis and its application for the production of D-mannose and L-ribose.AMB Express · 2019Article
- Engineering the l-Arabinose Isomerase from Enterococcus Faecium for d-Tagatose Synthesis.Molecules (Basel, Switzerland) · 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
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Authors and funding
2 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Bacillus coagulans has been of great commercial interest over the past decade owing to its strong ability of producing optical pure L: -lactic acid from both hexose and pentose sugars including L: -arabinose with high yield, titer and productivity under thermophilic conditions. The L: -arabinose isomerase (L-AI) from Bacillus coagulans was heterologously over-expressed in Escherichia coli. The open reading frame of the L-AI has 1,422 nucleotides encoding a protein with 474 amino acid residues. The recombinant L-AI was purified to homogeneity by one-step His-tag affinity chromatography. The molecular mass of the enzyme was estimated to be 56 kDa by SDS-PAGE. The enzyme was most active at 70°C and pH 7.0. The metal ion Mn(2+) was shown to be the best activator for enzymatic activity and thermostability. The enzyme showed higher activity at acidic pH than at alkaline pH. The kinetic studies showed that the K (m), V (max) and k (cat)/K (m) for the conversion of L: -arabinose were 106 mM, 84 U/mg and 34.5 mM(-1)min(-1), respectively. The equilibrium ratio of L: -arabinose to L: -ribulose was 78:22 under optimal conditions. L: -ribulose (97 g/L) was obtained from 500 g/l of L: -arabinose catalyzed by the enzyme (8.3 U/mL) under the optimal conditions within 1.5 h, giving at a substrate conversion of 19.4% and a production rate of 65 g L(-1) h(-1).
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