ISSN: 0973-7510
E-ISSN: 2581-690X
L-asparaginase (E.C.3.5.1.1) enzyme was purified to homogeneity from Pseudomonas aeruginosa. In this study, investigation, partial purification and characterization of L-asparaginase enzyme from a Pseudomonas aeruginosa strain was studied by using different analytical approach. After screening for the presence of L-asparaginase activity in Pseudomonas aeruginosa strain which was isolated from soil, it was decided to choose intracellular enzyme sample for characterization and purification studies. Strain improvement of the production strain by chemical and UV mutagenesis. The optimum pH range for activity of L-asparaginase was alkaline pH ranges, about pH 8.0. The optimum temperature was dedicated as 40 OC. The molecular weight of L-asparaginase was determined Protein profiling by SDS PAGE as revealed the activity responsive protein bands were appeared on gel (160 kDa). The influence of the enzyme based on the certain physical and chemical characteristics.
L-asparaginase, Pseudomonas aeruginosa, enzyme, Mutagenesis
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