• V.D.Sarwade
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An attempt was made to purify the chromate reductase from an alkaliphile with 46 fold purification with 40 percent recovery. The molecular weight was found to be 20 kDa. The higher enzyme activity was observed at pH 7.5 to 8.5 and temperature 350C to 50 0C with K2Cr2O7 as a substrate. The thermal stability of chromate reductase was up to 700C. Metal ions have no significant inhibitory action on chromate reductase. No activity was observed at 80 0C during enzyme stability experiments. It was an interesting thing observed in this regard was the enzyme also shown nitro reductase activity. Km value is 0.065 and the Vmax is 0.3 indicating its high affinity towards potassium dichromate.

Chromate reductase, Nitroreductase, Pseudomonas DL17, Purification, xenobiotics

"Partial purification of chromate reductase from an Alkaliphile Pseudomonas DL17 (JN595813.1)", International Journal of Emerging Technologies and Innovative Research (www.jetir.org), ISSN:2349-5162, Vol.7, Issue 10, page no.3054-3065, October-2020, Available :http://www.jetir.org/papers/JETIR2010400.pdf

"Partial purification of chromate reductase from an Alkaliphile Pseudomonas DL17 (JN595813.1)", International Journal of Emerging Technologies and Innovative Research (www.jetir.org | UGC and issn Approved), ISSN:2349-5162, Vol.7, Issue 10, page no. pp3054-3065, October-2020, Available at : http://www.jetir.org/papers/JETIR2010400.pdf