Molecular characterization of the glucose isomerase from the thermophilic bacteriumFervidobacterium gondwanense
| Autor: | W.M. de Vos, A.C.M. Geerling, Jurrit Zeilstra, J. van der Oost, Leon Kluskens |
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| Rok vydání: | 2010 |
| Předmět: |
Xylose isomerase
Glucose-6-phosphate isomerase purification cloning medicine.disease_cause Microbiology thermotoga-neapolitana fructose Gram-Negative Anaerobic Straight Curved and Helical Rods Bacterial Proteins Microbiologie expression medicine biochemical-characterization Environmental Chemistry Corporate Staff Concernstaf Cloning Molecular Waste Management and Disposal Escherichia coli Aldose-Ketose Isomerases Phylogeny VLAG Water Science and Technology Thermostability biology Thermophile thermus-thermophilus General Medicine Thermus thermophilus biology.organism_classification Recombinant Proteins thermostability Blotting Southern Kinetics Biochemistry Genes Bacterial Thermotoga maritima d-xylose isomerase escherichia-coli bacteria Electrophoresis Polyacrylamide Gel Thermotoga neapolitana Half-Life |
| Zdroj: | Environmental Technology 31 (2010) 10 Environmental Technology, 31(10), 1083-1090 |
| ISSN: | 1479-487X 0959-3330 |
| DOI: | 10.1080/09593330903486673 |
| Popis: | The gene coding for xylose isomerase from the thermophilic bacterium Fervidobacterium gondwanense was cloned and overexpressed in Escherichia coli. The produced xylose isomerase (XylA), which closely resembles counterparts from Thermotoga maritima and T. neapolitana, was purified and characterized. It is optimally active at 70 degrees C, pH 7.3, with a specific activity of 15.0 U/mg for the interconversion of glucose to fructose. When compared with T. maritima XylA at 85 degrees C, a higher catalytic efficiency was observed. Divalent metal ions Co2+ and Mg2+ were found to enhance the thermostability. |
| Databáze: | OpenAIRE |
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