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Transgenic expression of glucose dehydrogenase in Azotobacter vinelandii enhances mineral phosphate solubilization and growth of sorghum seedlings

The enzyme quinoprotein glucose dehydrogenase (GDH) catalyses the oxidation of glucose to gluconic acid by direct oxidation in the periplasmic space of several Gram‐negative bacteria. Acidification of the external environment with the release of gluconic acid contributes to the solubilization of the...

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Detalles Bibliográficos
Autores principales: Sashidhar, Burla, Podile, Appa Rao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815912/
https://www.ncbi.nlm.nih.gov/pubmed/21255283
http://dx.doi.org/10.1111/j.1751-7915.2009.00119.x
Descripción
Sumario:The enzyme quinoprotein glucose dehydrogenase (GDH) catalyses the oxidation of glucose to gluconic acid by direct oxidation in the periplasmic space of several Gram‐negative bacteria. Acidification of the external environment with the release of gluconic acid contributes to the solubilization of the inorganic phosphate by biofertilizer strains of the phosphate‐solubilizing bacteria. Glucose dehydrogenase (gcd) gene from Escherichia coli, and Azotobacter‐specific glutamine synthetase (glnA) and phosphate transport system (pts) promoters were isolated using sequence‐specific primers in a PCR‐based approach. Escherichia coli gcd, cloned under the control of glnA and pts promoters, was mobilized into Azotobacter vinelandii AvOP and expressed. Sorghum seeds were bacterized with the transgenic azotobacters and raised in earthen pots in green house. The transgenic azotobacters, expressing E. coli gcd, showed improved biofertilizer potential in terms of mineral phosphate solubilization and plant growth‐promoting activity with a small reduction in nitrogen fixation ability.