Prof. Dr. Appa Rao Podile
University of Hyderabad
Department of Plant Sciences
Hyderabad - 500046
India
Professor Appa Rao Podile has over two decades of research experience in plant microbe interactions. So far, six students obtained Ph.D. and four students obtained M. Phil. under the guidance of Prof. Podile at University of Hyderabad. Prof. Podile started his research career working on the plant cell wall degrading enzymes produced by vascular wilt pathogens and also with the proteins associated with plant cell walls and their role in immobilization/inactivation of pathogen-produced enzymes. Subsequently, Prof. Podile has been working on two important enzymes produced by plant-associated bacteria. Prof. Podile’s group worked on the importance of chitin-degradation by chitinolytic bacteria in biological control of plant pathogenic fungi. Further, Prof. Podile’s lab is interested in the glucose oxidation pathway directly by the glucose dehydrogenase by mineral phosphate solubilizing bacteria. Prof. Podile’s lab cloned the genes that code for chitinases and glucose dehyrogenase of Serratia marcesans. Using a site-directed mutagenesis (SDM) approach Prof. Podile’s lab modified the substrate affinity, and EDTA and temperature tolerance of glucose dehydrogenase. Currently work is under progress to clone more genes involved in chitinolysis by plant associated bacteria, characterization of the enzymes and also to modify the properties of chitinases using SDM.
In a collaboration with Prof. Dr. Bruno Moerschbacher from the University of Münster, financially supported by a DAAD/DST grant, Prof. Podile is assessing the potential of chitinolytic plant growth promoting rhizobacteria and chitosan for alternative, low-cost, environment-friendly and consumer-safe plant disease protection.
Prof. Podile is also a member of the NBS-TTC consortium which enlarges and supports the consortium of the ongoing European research project NanoBioSaccharides coordinated by Prof. Moerschbacher. In this project, the group of Prof. Podile will be responsible for the site directed mutagenesis of chitinases with an aim to change the substrate specificities and/or product patterns of these enzymes.
