The tannase enzyme was produced by the bacterial strain Enterobacter hormaechei Z8B-60 isolated from the slaughterhouse waste soil. Maximum tannase has been produced under ideal circumstances in a selective medium made of MSM-tannic acid as a sole carbon source. Ion exchange chromatography was used to partially purify the tannase using DEAE-cellulose. With a yield of 37.39% and a total purification of 21.23fold, purified tannase exhibited a specific activity of 24.864 U/mg. The enzyme that had been largely purified displayed an optimal pH of 6.5 and a temperature range of 50oC. The enzyme was stable up to 60oC and was most stable at a pH of 6.5. The purified enzyme displayed Km and Vmax values for methyl gallate of 9.268928mM and 0.667646U/mL and for propyl gallate of 6.818419mM and 0.180015U/mL, respectively. Ten mmol/L concentrations of Zn2+ and Co2+ were shown to stabilize tannase activity, whereas Mn2+, Fe2+ and Cu2+ inhibit tannase activity.