The present work describes purification and characterization of an extracellular cellulase from a newly isolated cellulolytic bacterial strain Bacillus pumilus EWBCM1. The candidate strain was tested for its abilities to hydrolyze the structural polysaccharides through the depolymerising activities of carboxymethylcellulase. The purification of cellulase was carried out by ammonium sulphate precipitation, DEAE cellulose and sephadex G-100. Purified cellulase was found to be 47.56 fold along with 1.46 U/mg of protein and the molecular weight of cellulase was 47 kDa through SDS-PAGE electrophoresis. The optimum activity of cellulase was registered at pH 10 at 50 °C. In the present study, metal ions inferred the addition of 5 mM CaCl₂ (128%) was recorded good activity than the other tested metal ions. Maximum activity of purified cellulase was recorded in 3% of NaCl and 5% of surfactants medium. The bioactive of purified cellulase was carried out with various commercial detergent and antimicrobial activity.

本工作描述了从新分离的纤维素分解细菌菌株短小芽孢杆菌EWBCM1纯化和表征细胞外纤维素酶。测试了候选菌株通过羧甲基纤维素酶的解聚活性水解结构多糖的能力。纤维素酶的纯化通过硫酸铵沉淀，DEAE纤维素和sephadex G-100进行。通过SDS-PAGE电泳，发现纯化的纤维素酶与1.46U / mg蛋白质一起为47.56倍，并且纤维素酶的分子量为47kDa。纤维素酶的最佳活性在50°C的pH 10下记录。在本研究中，金属离子推断添加了5 mM CaCl ₂（128％）具有比其他测试金属离子更高的活性。在3％的NaCl和5％的表面活性剂培养基中记录了纯化纤维素酶的最大活性。纯化的纤维素酶的生物活性用各种商业洗涤剂和抗菌活性进行。