ArticlePloS one2018
Biochemical properties of L-arabinose isomerase from Clostridium hylemonae to produce D-tagatose as a functional sweetener.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 37 citations in OpenAlex.
- Expression and Characterization of L-Arabinose Isomerase and Its Enzymatic Recycling of the Expired Milk.Foods (Basel, Switzerland) · 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
- Exploring a Highly D-Galactose Specific L-Arabinose Isomerase FromFrontiers in bioengineering and biotechnology · 2020Article
- Characterization of a D-lyxose isomerase from Bacillus velezensis and its application for the production of D-mannose and L-ribose.AMB Express · 2019Article
- Overcoming the thermodynamic equilibrium of an isomerization reaction through oxidoreductive reactions for biotransformation.Nature communications · 2019Article
- Enzymatic synthesis of l-fucose from l-fuculose using a fucose isomerase fromBiotechnology for biofuels · 2019Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
d-Tagatose has gained substantial interest due to its potential functionalities as a sucrose substitute. In this study, the gene araA, encoding l-arabinose isomerase (l-AI) from Clostridium hylemonae (DSM 15053), was cloned and expressed in Escherichia coli BL21 (DE3). This gene consists of 1,506 nucleotides and encodes a protein of 501 amino acid residues with a calculated molecular mass of 56,554 Da. Since l-AI was expressed as an intracellular inclusion body, this enzyme was solubilized with guanidine hydrochloride, refolded, and activated with a descending concentration gradient of urea. The purified enzyme exhibited the greatest activity at 50°C, pH 7-7.5, and required 1 mM of Mg2+ as a cofactor. Notably, the catalytic efficiency (3.69 mM-1sec-1) of l-AI from C. hylemonae on galactose was significantly greater than that of other previously reported enzymes. The bioconversion yield of d-tagatose using the C. hylemonae l-arabinose isomerase at 60°C reached approximately 46% from 10 mM of d-galactose after 2 h. From these results, it is suggested that the l-arabinose isomerase from C. hylemonae could be utilized as a potential enzyme for d-tagatose production due to its high conversion yield at an industrially competitive temperature.
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