10.22376/ijpbs.2019.10.1.p1-12 Volume 5 Issue 1 2014 (January - March) The extremely halophilic archaeon lessThan i greaterThan Natrinema sp. lessThan /i greaterThan strain SSBJUP-1, which produces extracellular cellulase and xylanase, was isolated from the Lonar Lake situated in Buldhana, Maharashtra. The enzymes were optimally active at pH 9–10 and temperature 40–60 lessThan sup greaterThan 0 lessThan /sup greaterThan C and they were most stable up to pH 11 and 16 % of NaCl concentration. The xylanase showed maximum activity at 50 lessThan sup greaterThan 0 lessThan /sup greaterThan C and cellulase at 40 lessThan sup greaterThan 0 lessThan /sup greaterThan C. Xylanase kept excellent activity over a broad range of salt concentration from 12 to 22% with highest activity at 16 % NaCl while Cellulase showed maximum activity at 14% of salt. Unlike xylanase that was stimulated by Cu lessThan sup greaterThan 2+ lessThan /sup greaterThan , Mg lessThan sup greaterThan 2+ lessThan /sup greaterThan and Ca lessThan sup greaterThan 2+ lessThan /sup greaterThan , cellulase activity was reduced when treated with Hg lessThan sup greaterThan 2+ lessThan /sup greaterThan and Cu lessThan sup greaterThan 2+ lessThan /sup greaterThan and stimulated by Mg lessThan sup greaterThan 2+ lessThan /sup greaterThan and Ca lessThan sup greaterThan 2+. lessThan /sup greaterThan This investigation showed that lessThan i greaterThan Natrinema sp. lessThan /i greaterThan strain SSBJUP-1 is a potential source of xylanase and cellulase and an interesting candidate for application in biotechnological processes. J. U. PATIL AND S. S. BAJEKAL Archaea, Haloalkaliphiles, Xylanase, Cellulase, Natrinema sp. 553-559