The present research investigation reports an attempt to optimize the reaction conditions for maximum activity of crude xylanase from Pseudomonas sp. XPB-16. Buffer system, pH, buffer molarity, reaction temperature, incubation time & substrate concentration were the main parameters that were optimized. Furthermore the influence of various metal ions and inhibitors on activity of enzyme was also assessed. Potassium phosphate buffer (50mM), pH 7.0 was reported as the most appropriate for maximal activity of xylanase amongst various buffers tested. The optimum temperature, incubation time, substrate concentration recorded for maximum xylanase activity were 37°C, 25 minutes, 0.6% (w/v) respectively. Sodium azide was reported as the most potent inhibitor of xylanase activity amongst various metal ions and inhibitors. The perspectives of xylan hydrolysis by xylanase from Pseudomonas sp. XPB-16 look quite promising. Thus future studies to enhance the xylan hydrolysis rate as well as to assure enhanced process control for increased activity of xylanase would be envisaged.
