For evaluating the relative effects of some polluting salts on the measurement of cellulase activity assayed by 3,5-dinitrosalicylate (DNS) this study was done. Glucose were the most effective inhibitors of cellulase activity. These ions inhibited exoglucanase more than endoglucanase. The effect of most ions on cellulase activity may be related to negative or positive effect of them on the method of cellulase assessment. So, for a better data interpretation in the study of ion effects on the soil enzyme activity, both the effects of ions on the method of enzyme assay, and the effects of ions on the enzyme activity should be studied. @JASEM Cellulase is an enzyme system that degrades cellulose and releases reducing sugars as the end products. The system consists of endo-l,4-B-glucanase (EC3.2.1.4), exo-I,4-B-glucanase (EC 3.2.1.91) and B-Dglucosidase (EC 3.2.1.21). Endo-α -1,4-glucanase (1,4-α-D-glucan-4-glucan-hydrolase) has the role of randomly degrading α-1,4-glucosidic bonds from the middle of the cellulose molecule. It does not attack cellobiose but hydrolyzes cellodextrines and substituted celluloses, for instance carboxymethylcellulose. Its specificity is moderate, different sub-types having various affinities for different length oligosaccharides. Exo-β-1,4-glucanase (1,4-β -D-glucan cellobiohydrolase) cuts step by step cellobiose units from the non-reducing end of cellulosic chains. It hydrolyses the cellodextrines but not the cellobiose. Its substrate specificity is rather high enabling it to degrade more than 80% from the crystalline cellulose while its degree of activity is different for different microorganisms.