IJCRRI Journ Cur Res ReInternational Journal of Current Research and ReviewI Journ Cur Res Re2231-21960975-5241Radiance Research Academy1993General SciencesPARTIAL PURIFICATION AND CHARACTERIZATION OF DETERGENT TOLERANT CELLULASE FROM BACILLUS SP. KP8 KushwahaDhairyawantKumarHarsh DevKGireesh Babu29092012)3137This article is copyright of Popeye Publishing, 20092009This is an open-access article distributed under the terms of the Creative Commons Attribution (CC BY 4.0) Licence. You may share and adapt the material, but must give appropriate credit to the source, provide a link to the licence, and indicate if changes were made.

In this study cellulase producing Bacillus sp. KP8 was isolated from soil. The crude cellulase was found to possess 0.012__ampersandsignmu;moles/ml/min activity. The purification using Sephadex G-100 and DEAE-Cellulose lead to ~189 fold purity with 9.09% recovery. The enzyme was found to be optimally active at pH 5.0, 45__ampersandsignordm;C. The partially purified fraction displayed two proteins of ~45 kD. The kinetic studies revealed a Km of 2.85, while the Vmax was found to be 5.9. The non-metallo cellulase was detergent stable, possessing serine at its active site, sensitive to the presence of Mg+2, Mn+2, Hg+2, Cu+2, H2O2 and NaCl.

Cellulase Bacillus sp. KP8 Sephadex G-100 DEAE-Cellulose SDS-PAGE