VARIABILITY IN BIOCHEMICAL ACTIVITIES AND PROTEIN PROFILES OF RHIZOBILIM ISOLATES FROM SESBANIA SPECIESM. SIUDEVI AND K. V. MALLAIAHAbstract Rhizobium strains from root and stem nodules of Sesbania species were isolated and studied for biochemical activities and protein profiles. It was observed that the Rhizobium isolates of Sesbania species showed wide variation in tryptophanase, protease, nitrate reductase, lysine decarboxylase, amylase, urease and citrase activities. None of the isolates produced gelatinase, caseinase, lipase, phenylalanine deaminase and DNase activities. The isolate from root nodules of S. procumbens (SPR) has the ability to solubilize the insoluble tricalcium phosphate. The isolates viz; SRR, SPR, SGR and SSR produced IAA in the culture medium. Analysis of total cellular proteins of Rhizobium isolates indicate that the banding pattern of SGR, SPR, SPS and SRS is almost similar, while the Rhizobium isolate from S. aculeata (SAR) is distinctly different from other isolates of Sesbania species.
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