Characterization of Crude Cellulase Enzyme Produced by Bacillus licheniformis P12 Isolate
Sudarma Dita Wijayanti, Kiki Oliviani, Joni Kusnadi, Rhytia Ayu C.P
Department of Agricultural Product Technology – Faculty of Agricultural Technology – Universitas Brawijaya
Abstract
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
Keywords: Bacillus licheniformis, Cellulase, fractionation
Topic: INDUSTRIAL BIOTECHNOLOGY AND BIOPROCESSING