ArticleJournal of agricultural and food chemistry2014
L-Arabinose isomerase and D-xylose isomerase from Lactobacillus reuteri: characterization, coexpression in the food grade host Lactobacillus plantarum, and application in the conversion of D-galactose and D-glucose.
Article in Journal of agricultural and food chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 56 citations in OpenAlex.
- A recombinant xylose reductase enzyme with biotechnological potential for xylitol production.Archives of microbiology · 2026Article
- Recombinant production of acidophilic L-arabinose isomerase from Lentilactobacillus parakefiri in Bacillus subtilis.Microbial cell factories · 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
- Effect of Coix Seed Extracts on Growth and Metabolism ofFoods (Basel, Switzerland) · 2022Article
- Pentose degradation in archaea: Halorhabdus species degrade D-xylose, L-arabinose and D-ribose via bacterial-type pathways.Extremophiles : life under extreme conditions · 2020Article
- Article
- Purification and kinetic behavior of glucose isomerase fromSaudi journal of biological sciences · 2020Article
- Protective effects of a food-grade recombinant Lactobacillus plantarum with surface displayed AMA1 and EtMIC2 proteins of Eimeria tenella in broiler chickens.Microbial cell factories · 2020Article
- Production, purification and physicochemical characterization of D-xylose/glucose isomerase from3 Biotech · 2020Article
- 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
- Overcoming the thermodynamic equilibrium of an isomerization reaction through oxidoreductive reactions for biotransformation.Nature communications · 2019Article
- β-Galactosidase fromInternational journal of molecular sciences · 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
- Metal Dependence of the Xylose Isomerase from Piromyces sp. E2 Explored by Activity Profiling and Protein Crystallography.Biochemistry · 2017Article
- Cloning, Expression, and Characterization of a Novel L-Arabinose Isomerase from the Psychrotolerant Bacterium Pseudoalteromonas haloplanktis.Molecular biotechnology · 2016Article
- Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Secretory production of a beta-mannanase and a chitosanase using a Lactobacillus plantarum expression system.Microbial cell factories · 2016Article
- Tuning constitutive recombinant gene expression in Lactobacillus plantarum.Microbial cell factories · 2014Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
The L-arabinose isomerase (L-AI) and the D-xylose isomerase (D-XI) encoding genes from Lactobacillus reuteri (DSMZ 17509) were cloned and overexpressed in Escherichia coli BL21 (DE3). The proteins were purified to homogeneity by one-step affinity chromatography and characterized biochemically. L-AI displayed maximum activity at 65 °C and pH 6.0, whereas D-XI showed maximum activity at 65 °C and pH 5.0. Both enzymes require divalent metal ions. The genes were also ligated into the inducible lactobacillal expression vectors pSIP409 and pSIP609, the latter containing a food grade auxotrophy marker instead of an antibiotic resistance marker, and the L-AI- and D-XI-encoding sequences/genes were coexpressed in the food grade host Lactobacillus plantarum . The recombinant enzymes were tested for applications in carbohydrate conversion reactions of industrial relevance. The purified L-AI converted D-galactose to D-tagatose with a maximum conversion rate of 35%, and the D-XI isomerized D-glucose to D-fructose with a maximum conversion rate of 48% at 60 °C.
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