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- Publisher
- Springer Journals
- Copyright
- Copyright © 2007 by Association of Microbiologists of India
- Subject
- Life Sciences; Medical Microbiology ; Microbiology
- ISSN
- 0046-8991
- eISSN
- 0973-7715
- DOI
- 10.1007/s12088-007-0025-7
- pmid
- 23100654
- Publisher site
- See Article on Publisher Site
Abstract
Glucose dehydrogenase (GDH) of Gram-negative bacteria is a membrane bound enzyme catalyzing the oxidation of glucose to gluconic acid and is involved in the solubilization of insoluble mineral phosphate complexes. A 2.4 kb glucose dehydrogenase gene (gcd) of Enterobacter asburiae sharing extensive homology to the gcd of other enterobacteriaceae members was cloned in a PCR-based directional genome walking approach and the expression confirmed in Escherichia coli YU423 on both MacConkey glucose agar and hydroxyapatite (HAP) containing media. Mineral phosphate solubilization by the cloned E. asburiae gcd was confirmed by the release of significant amount of phosphate in HAP containing liquid medium. gcd was over expressed in E. coli AT15 (gcd::cm) and the purified recombinant protein had a high affinity to glucose, and oxidized galactose and maltose with lower affinities.
Journal
Indian Journal of Microbiology – Springer Journals
Published: Jul 8, 2007