ArticleBMC biotechnology2016
Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production.
Article in BMC biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 49 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
- Reversal of the Leloir pathway to promote galactose and tagatose synthesis from glucose.Cell reports. Physical science · 2025Article
- Transforming monosaccharides: Recent advances in rare sugar production and future exploration.BBA advances · 2025Article
- Development and Characterization of a Tunable Metal-Organic Framework (MOF) for the Synthesis of a Rare Sugar D-Tagatose.Applied biochemistry and biotechnology · 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
- 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
- Galactose to tagatose isomerization at moderate temperatures with high conversion and productivity.Nature communications · 2019Article
- Characterization of a D-lyxose isomerase from Bacillus velezensis and its application for the production of D-mannose and L-ribose.AMB Express · 2019Article
- D-Tagatose Is a Promising Sweetener to Control Glycaemia: A New Functional Food.BioMed research international · 2018Review
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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
backgroundL-arabinose isomerase (AI) is a crucial catalyst for the biotransformation of D-galactose to D-tagatose. In previous reports, AIs from thermophilic bacterial strains had been wildly researched, but the browning reaction and by-products formed at high temperatures restricted their applications. By contrast, AIs from mesophilic Bacillus strains have some different features including lower optimal temperatures and lower requirements of metallic cofactors. These characters will be beneficial to the development of a more energy-efficient and safer production process. However, the relevant data about the kinetics and reaction properties of Bacillus AIs in D-tagatose production are still insufficient. Thus, in order to support further applications of these AIs, a comprehensive characterization of a Bacillus AI is needed.
resultsThe coding gene (1422 bp) of Bacillus coagulans NL01 AI (BCAI) was cloned and overexpressed in the Escherichia coli BL21 (DE3) strain. The enzymatic property test showed that the optimal temperature and pH of BCAI were 60 °C and 7.5 respectively. The raw purified BCAI originally showed high activity in absence of outsourcing metallic ions and its thermostability did not change in a low concentration (0.5 mM) of Mn(2+) at temperatures from 70 °C to 90 °C. Besides these, the catalytic efficiencies (k cat/K m) for L-arabinose and D-galactose were 8.7 mM(-1) min(-1) and 1.0 mM(-1) min(-1) respectively. Under optimal conditions, the recombinant E. coli cell containing BCAI could convert 150 g L(-1) and 250 g L(-1) D-galactose to D-tagatose with attractive conversion rates of 32 % (32 h) and 27 % (48 h).
conclusionsIn this study, a novel AI from B. coagulans NL01was cloned, purified and characterized. Compared with other reported AIs, this AI could retain high proportions of activity at a broader range of temperatures and was less dependent on metallic cofactors such as Mn(2+). Its substrate specificity was understood deeply by carrying out molecular modelling and docking studies. When the recombinant E. coli expressing the AI was used as a biocatalyst, D-tagatose could be produced efficiently in a simple one-pot biotransformation system.
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