Warning: ini_set(): A session is active. You cannot change the session module's ini settings at this time in /home/updatepublishing/public_html/journal/lib/pkp/classes/session/SessionManager.inc.php on line 69

Warning: Cannot modify header information - headers already sent by (output started at /home/updatepublishing/public_html/journal/lib/pkp/classes/session/SessionManager.inc.php:69) in /home/updatepublishing/public_html/journal/plugins/generic/citationStyleLanguage/CitationStyleLanguagePlugin.inc.php on line 478

Warning: Cannot modify header information - headers already sent by (output started at /home/updatepublishing/public_html/journal/lib/pkp/classes/session/SessionManager.inc.php:69) in /home/updatepublishing/public_html/journal/plugins/generic/citationStyleLanguage/CitationStyleLanguagePlugin.inc.php on line 479
TY - JOUR AU - Hauli, Ipsit AU - Sarkar, Bidisha AU - Mukherjee, Trinetra AU - Mukhopadhyay, Subhra Kanti PY - 2013/09/11 Y2 - 2025/09/23 TI - Purification and characterization of a thermoalkaline, cellulase free thermostable xylanase from a newly isolated Anoxybacillus sp. Ip-C from hot spring of Ladakh JF - Research in Biotechnology JA - RIB VL - 4 IS - 4 SE - Research Articles DO - UR - https://www.updatepublishing.com/journal/index.php/rib/article/view/2438 SP - AB - <p>An alkaline, highly thermostable cellulase free xylanase was purified from a thermophilic <em>Anoxybacillus</em> sp. Ip-C, newly isolated from hot spring of Ladakh. The enzyme was purified using ammonia sulphate precipitation followed by Sephadex G-75. The molecular weight of the xylanase was about 45 kDa, as analyzed by SDS-PAGE. The enzyme had optimum activity at pH 9.0 and 70ºC temperature; the enzyme retained 90% of its original activity for 96 hrs at 70 ºC. V_max and K_m of the enzyme were found to be 13.5 µmol min^-1 mg^-1 protein and 4.59 mg ml^-1, respectively. Metal ions, Ca⁺², Fe⁺² and Mg⁺² highly enhance the enzyme activity to 122.45, 119.06 and 118.98% respectively; whereas SDS and Hg⁺² completely inhibit (0 U/ml) the enzyme activity. TLC analysis of enzymatic hydrolysis products showed that this xylanase is an endoxylanase, and generates xylooligosaccharides. Thus, it provides a potential thermostable alkaline xylanase for industrial applications.</p> ER -