Isolation, Characterization and Purification of an Extracellular Enzyme Agarase from Agarolytic bacteria

In the present study the bacteria are isolate from soil samples. On screening of the samples for agar-degrading, were found to contain agarolytic bacteria. In each sample, various patterns of agar degradation were seen indicating different bacteria present in the sample. Different isolates were found all are gram negative they were checked for reproducibility of the agarolytic activity by culturing on the capex dox media. They were identified to be rod shaped. The strain was susceptible to penicillin, kanamycin and reactive to cloistin. An enzyme, agarase has purified appears to release oligosaccharide units, but not free galactose, from agar. Therefore, it is evident that the agarase specifically cleaves β- I, 4 linkages between D-galactose and 3, 6-anhydro-lactose of the agarose structure. The enzyme had a specific agarase activity with 1% agar and 0.1% galactose. The enzyme activity of 0.1 % galactose gradually increases as purification step and the enzyme activity of 1 % agar gradually decreases as purification step.