Indian Journal of Microbiology

, Volume 47, Issue 2, pp 126–131 | Cite as

Glucose dehydrogenase of a rhizobacterial strain of Enterobacter asburiae involved in mineral phosphate solubilization shares properties and sequence homology with other members of enterobacteriaceae

  • C. Tripura
  • P. Sudhakar Reddy
  • M. K. Reddy
  • B. Sashidhar
  • A. R. Podile
Original Article


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.

The enzyme was highly sensitive to heat and EDTA, and belonged to Type I, similar to GDH of E. coli.


Enterobacter asburiae Glucose dehydrogenase Mineral phosphate solubilization 


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Copyright information

© Association of Microbiologists of India 2007

Authors and Affiliations

  • C. Tripura
    • 1
  • P. Sudhakar Reddy
    • 2
  • M. K. Reddy
    • 2
  • B. Sashidhar
    • 1
  • A. R. Podile
    • 1
  1. 1.Department of Plant SciencesUniversity of Hyderabad, P. O. Central UniversityHyderabadIndia
  2. 2.International Centre for Genetic Engineering and Biotechnology (ICGEB)New DelhiIndia

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