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Cellulase obtained from Bacillus subtilis ITBCCB148 has successfully been isolated and purified. The native enzyme was modified with dimethyladipimidate (DMA) to increase the stability of the enzyme. The native and modified enzymes were characterized including determination of optimum temperature, optimum pH and thermal stability. The activity of the cellulase was determined based on Mendels method and the protein content was determined based on Lowry method. The results showed that the native enzyme has optimum temperature of 55oC and optimum pH of 5.5. The thermal stability for 60 minutes at temperature of 55oC indicated that the native enzyme has ki = 0.034 min.t-1, t1/2 = 20.4 min., and ΔGi = 100.9 kJ/mol. The modified enzyme with modification degrees of 64.5; 69.5 and 82% have optimum temperature of 55 oC and optimum pH of 6. The thermal stability for 60 minutes at temperature of 55oC of the modified enzyme with modification degrees of 64.5; 69.5 and 82% have ki values of 0.024; 0.021 and 0.022 min.- 1, t1/2 values of 28.9; 33.0 and 31.5 minutes, and ΔGi values of 101.9; 102.3 and 102.2 kJ/ mol, respectively. The modification with DMA has successfully increased the thermal stability of the modified enzymes between 1.4 – 1.6 times compared to that of the native enzyme. The decrease of ki values, increase of half-lives and ΔGi indicated that the modified enzymes were more stable compared to the native enzyme.

The Chemical Modification of Cellulase Obtained from Bacillus subtilis ITBCCB148 With Dimethyladimipidate