Ontology highlight
ABSTRACT: Background
L-asparaginase has been used as a chemotherapeutic agent in treatment of lymphoblastic leukemia. In the present investigation, Bacillus sp. PG03 and Bacillus sp. PG04 were studied.Methods
L- asparaginases were produced using different culture media and were purified using ion exchange chromatography.Results
Maximum productivity was obtained when asparagine was used as the nitrogen source at pH 7 and 48 h after cultivation. New intracellular L-asparaginases showed an apparent molecular weight of 25 kDa and 30 kDa by SDS-PAGE respectively. These enzymes were active in a wide pH range (3-9) with maximum activity at pH 6 for Bacillus PG03 and pH 7 for Bacillus PG04 L-asparaginase. Bacillus PG03 enzyme was optimally active at 37 ˚C and Bacillus PG04 maximum activity was observed at 40˚C. Kinetic parameters km and Vmax of both enzymes were studied using L-asparagine as the substrate. Thermal inactivation studies of Bacillus PG03 and Bacillus PG04 L-asparaginase exhibited t1/2 of 69.3 min and 34.6 min in 37 ˚C respectively. Also T50 and ∆G of inactivation were measured for both enzymes.Conclusion
The results revealed that both enzymes had appropriate characteristics and thus could be a potential candidate for medical applications.
SUBMITTER: Rahimzadeh M
PROVIDER: S-EPMC5144114 | biostudies-literature | 2016
REPOSITORIES: biostudies-literature
The open biochemistry journal 20161104
<h4>Background</h4>L-asparaginase has been used as a chemotherapeutic agent in treatment of lymphoblastic leukemia. In the present investigation, <i>Bacillus</i> sp. PG03 and <i>Bacillus</i> sp. PG04 were studied.<h4>Methods</h4>L- asparaginases were produced using different culture media and were purified using ion exchange chromatography.<h4>Results</h4>Maximum productivity was obtained when asparagine was used as the nitrogen source at pH 7 and 48 h after cultivation. New intracellular L-aspa ...[more]