ArticleFrontiers in chemistry2020
Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From
Article in Frontiers in chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 37 citations in OpenAlex.
- Advances in erythritol production through synthetic biology and systems metabolic engineering.Archives of microbiology · 2026Review
- Potential and Challenges ofFoods (Basel, Switzerland) · 2025Review
- Enabling Stable Recycling of L-Arabinose Isomerase Through Whole-Cell Immobilization for Efficient and Cost-Effective D-Tagatose Production.Foods (Basel, Switzerland) · 2025Article
- Transforming monosaccharides: Recent advances in rare sugar production and future exploration.BBA advances · 2025Article
- Optimization of fermentation conditions for whole cell catalytic synthesis of D-allulose by engineering Escherichia coli.Scientific reports · 2024Article
- Comprehensive Analysis of Allulose Production: A Review and Update.Foods (Basel, Switzerland) · 2024Review
- Biochemical characterization, structure-guided mutagenesis, and application of a recombinant D-allulose 3-epimerase fromFrontiers in bioengineering and biotechnology · 2024Article
- The Characterization of a Novel D-allulose 3-Epimerase fromFoods (Basel, Switzerland) · 2022Article
- Research Advances of d-allulose: An Overview of Physiological Functions, Enzymatic Biotransformation Technologies, and Production Processes.Foods (Basel, Switzerland) · 2021Review
- D-Allulose 3-epimerase of Bacillus sp. origin manifests profuse heat-stability and noteworthy potential of D-fructose epimerization.Microbial cell factories · 2021Article
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8 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEase that works at acidic conditions is highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on -fructose at pH 6.0 and 50°C with a
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