Asian Journal of Microbiology, Biotechnology & Environmental Sciences Paper

Vol.14, Issue 1, 2012; Page No.(19-22)

EXTRACTION AND PURIFICATION OF NITROGENASE REDUCTASE ENZYME (FE PROTEIN) FROM RHIZOBIUM STRAIN

P. JAYALAKSHMI, P. SUVARNALATHA DEVI, *N.D. PRASANNA AND G. REVATHI

Abstract

Biological nitrogen fixation involves the reduction of atmospheric dinitrogen (N2) into ammonia (NH3) by a metalloenzyme nitrogenase. The nitrogenase reductase (Fe-protein) isolated from Rhizobium strain was been purified and characterized. The nitrogenase Fe protein is a a2 dimer containing Fe4S4 cluster. The Fe-protein is similar to other Fe-proteins with respect to its molecular weight. The Fe-protein was eluted with 400mM-Nacl on to a DEAE-cellulose column as a dark-brown band at the top of the column. The molecular weight of the protein is about 60 K .Da. and the protein concentration is about 14.2mg/mL.

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