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Xylan, being major hemicellulose and constituent of wood, is the second most abundant polysaccharide after cellulose. Xylan consisting of a linear backbone made of β-1, 4 linked xylose residues with side chains comprising various side groups. It is found in middle lamella of plant cell wall and forms an interface between lignin and other polysaccharides. Xylanases belong to hydrolytic enzymes, which catalyze the breakdown of xylan. It is produced by various types of microbes including fungi, bacteria and yeast. Xylan is receiving more attention these days because of its potential applications in improving digestibility of animal feed, bleaching and bioconversion of lignocelluloses into feed-stocks and fuels. Hence, this study was carried out to isolate potent bacteria from soil capable of producing xylanase. Soil samples were collected from different regions for isolating the potent xylanase producing bacteria. A total of 10 bacterial isolates were isolated from soil samples on selective medium. Primarily screened bacterial isolates were then subjected to secondary screening by flooding the plates with iodine solution, and four isolates showed zone of hydrolysis around them. Furthermore, these four bacterial isolates (A-5, C-4, F-2 and H-2) were selected for estimation of protein content and determination of amount of xylose liberated in culture filtrate as a result of hydrolysis of substrate. Protein contents in the culture filtrate of A-5, C-4, F-2 and H-2 were observed to be 2.5, 2.9, 2.19 and 2.87 mg/ml, respectively. The amount of xylose liberated in culture filtrate of A-5, C-4, F-2 and H-2 was estimated to be 1.29, 0.953, 1.577 and 1.358 mg/ml, respectively. Further the enzyme activity of isolates A-5, C-4, F-2 and H-2 was calculated to be 0.516 mg xylose liberated/mg protein/10 min at 55°C, 0.328 mg xylose liberated/mg protein/10 min at 55°C, 0.720 mg xylose liberated/mg protein/10 min at 55°C, 0.470 mg xylose liberated/mg protein/10 min at 55°C, 0.700 mg xylose liberated/mg protein/10 min at 55°C. In this way, isolate F-2 and A-S showed the best activity, A-5 showed moderate enzyme activity and isolates C-4 and H-2 showed the least xylanase activity.