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Microbial enzymes utilization in industrial application recently has become extensive. One enzyme that is widely used in industry is the cellulase which is able to hydrolyze the glycosidic B-1.4 bonds present in cellulose. In previous studies, isolation of a cellulose degrading bacteria P12 from Mount Merapi spring water was carried out which had the highest cellulolytic activity (2.326 ± 0.219 U/mg). This research aims to identify P12 isolates molecularly using the 16S-rRNA gene, and characterize the cellulase produced. A descriptive quantitative design was used in this research. The P12 isolate was revealed to be Bacillus licheniformis based on 16S rRNA analysis with 99% homology. The concentration of ammonium sulfate 70% saturation can precipitate cellulase enzymes with purification folds of 6 times with specific activities 0.0103 U / mg. Cellulase enzyme fractionated with ammonium sulfate at this research was optimum at pH 7 and temperature 50C