ArticleApplied and environmental microbiology2005
Characterization of the highly efficient sucrose isomerase from Pantoea dispersa UQ68J and cloning of the sucrose isomerase gene.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 89 citations in OpenAlex.
- Sucrose Isomerase Mutants' Expression inMicroorganisms · 2026Article
- Unraveling the genetic traits and functional diversity of the pan-genome in Pantoea dispersa.BMC genomics · 2025Article
- Article
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- Thermostability improvement of sucrose isomerase PalI NX-5: a comprehensive strategy.Biotechnology letters · 2023Article
- Enhancement of healthful novel sugar contents in genetically engineered sugarcane juice integrated with molecularly characterized ThSyGII (CEMB-SIG2).Scientific reports · 2022Article
- Enhanced Extracellular Production and Characterization of Sucrose Isomerase inFoods (Basel, Switzerland) · 2022Article
- Optimization and validation for quantification for allulose of jelly candies using response surface methodology.Journal of food science and technology · 2021Article
- Stem vacuole-targetted sucrose isomerase enhances sugar content in sorghum.Biotechnology for biofuels · 2021Article
- Engineering a Highly Active Sucrose Isomerase for Enhanced Product Specificity by Using a "Battleship" Strategy.Chembiochem : a European journal of chemical biology · 2020Article
- Display of a sucrose isomerase on the cell surface of3 Biotech · 2019Article
- Efficient Conversion of Cane Molasses Towards High-Purity Isomaltulose and Cellular Lipid Using an EngineeredMolecules (Basel, Switzerland) · 2019Article
- Enzymatic modification of daidzin using heterologously expressed amylosucrase inFood science and biotechnology · 2019Article
- Enhancing the Thermostability of Serratia plymuthica Sucrose Isomerase Using B-Factor-Directed Mutagenesis.PloS one · 2016Article
- Synthesis and characterization of polysaccharide-maghemite composite nanoparticles and their antibacterial properties.Nanoscale research letters · 2012Article
- Isomaltulose is actively metabolized in plant cells.Plant physiology · 2011Article
- Article
- Immobilization of Erwinia sp. D12 Cells in Alginate-Gelatin Matrix and Conversion of Sucrose into Isomaltulose Using Response Surface Methodology.Enzyme research · 2011Article
- Gene cloning, protein characterization, and alteration of product selectivity for the trehalulose hydrolase and trehalulose synthase from "Pseudomonas mesoacidophila" MX-45.Applied and environmental microbiology · 2009Article
- Isomaltose production by modification of the fructose-binding site on the basis of the predicted structure of sucrose isomerase from "Protaminobacter rubrum".Applied and environmental microbiology · 2008Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose isomerase (SI) genes from Pantoea dispersa UQ68J, Klebsiella planticola UQ14S, and Erwinia rhapontici WAC2928 were cloned and expressed in Escherichia coli. The predicted products of the UQ14S and WAC2928 genes were similar to known SIs. The UQ68J SI differed substantially, and it showed the highest isomaltulose-producing efficiency in E. coli cells. The purified recombinant WAC2928 SI was unstable, whereas purified UQ68J and UQ14S SIs were very stable. UQ68J SI activity was optimal at pH 5 and 30 to 35 degrees C, and it produced a high ratio of isomaltulose to trehalulose (>22:1) across its pH and temperature ranges for activity (pH 4 to 7 and 20 to 50 degrees C). In contrast, UQ14S SI showed optimal activity at pH 6 and 35 degrees C and produced a lower ratio of isomaltulose to trehalulose (<8:1) across its pH and temperature ranges for activity. UQ68J SI had much higher catalytic efficiency; the Km was 39.9 mM, the Vmax was 638 U mg(-1), and the Kcat/Km was 1.79 x 10(4) M(-1) s(-1), compared to a Km of 76.0 mM, a Vmax of 423 U mg(-1), and a Kcat/Km of 0.62 x 10(4) M(-1) s(-1) for UQ14S SI. UQ68J SI also showed no apparent reverse reaction producing glucose, fructose, or trehalulose from isomaltulose. These properties of the P. dispersa UQ68J enzyme are exceptional among purified SIs, and they indicate likely differences in the mechanism at the enzyme active site. They may favor the production of isomaltulose as an inhibitor of competing microbes in high-sucrose environments, and they are likely to be highly beneficial for industrial production of isomaltulose.
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