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An extracellular alkali-halotolerant cellulase from the strain Bacillus flexus NT isolated from Ulva lactuca was purified to homogeneity with a recovery of 25.03% and purity fold of 22.31. The molecular weight of the enzyme was about 97kDa and the V_max and K_m was 370.17U/ml/min and 6.18mg/ml respectively. The optimum pH and temperature for enzyme activity was 10 and 45°C respectively. The enzymatic hydrolysis of the CMC was confirmed with GPC and GC-MS analysis. The stabilized activity of the enzyme even at high pH of 9.0–12.0 and residual activity of about 70% at salt concentration (NaCl 15%) revealed for its alkali-halotolerance nature. The metal ions Cd²⁺ and Li¹⁺ were found as inducers while Cr²⁺, Co²⁺, Zn²⁺ and metal chelator EDTA have significantly inhibited the enzyme activity. Enzyme activity was insensitive to ethanol and isopropanol while partially inhibited by acetone, cyclohexane and …