Abstract
This study reports the cytotoxic potential of L-Asparaginase isolated from Bacillus sp. Bacillus sp. was isolated from local soil/water samples and identified by rapid plate assay and further confirmed by phenotypic characterization. Extracellular L- Asparaginase was isolated from broth culture of Bacillus sp. and purified by ammonium sulfate precipitation, followed by dialysis and ion exchange and gel filtration chromatography techniques. The purified enzyme was used to study the in vitro cytotoxic potential. Varying concentrations (31.25, 62.5, 125, 250, 500 µg/ml) of purified L-Asparaginase was tested on MCF7, HeLa, HepG2 and 3T3L1cell lines by MTT assay. Curcumin was maintained as a positive control. The results revealed that the enzyme showed a significant cytotoxic activity and a dose dependent effect. Minimum inhibition of (19.44%) was observed at an enzyme concentration of 31.25 µg/ml and maximum inhibition (71.14%) was observed at 500ug/ml against MCF7 cell line. Minimum inhibition of (10.04%) was observed at an enzyme concentration 31.25 µg/ml and maximum inhibition (68.92%) was observed at 500 µg/ml against HeLa cell line. Minimum inhibition of (7.45%) was shown at an enzyme concentration of 31.25 µg/ml and maximum inhibition (68.28 %) was observed at 500 µg/ml against HepG2 cell line. Minimum inhibition of (4.4%) was shown by enzyme concentration 31.25 µg/ml and maximum inhibition (47.4%) was observed at 500 µg/ml against 3T3L1 cell line. Curcumin at 5µM concentration showed an inhibition of 48.13% against MCF-7 cells, 54.42% against HeLa cells, 64.94% against HepG2 cells and 44.5% against 3T3L1 cell lines.
Highlights
Identification of the L-Asparaginase producing bacterial isolateL-asparaginase (L-asparagine amidohydrolase EC 3.5.1.1) is a hydrolase that plays a major role in the metabolism of all living organisms catalyzing the hydrolysis of L-asparagine to L-aspartic acid and ammonia (Lincoln and More, 2014)
This study reports the cytotoxic potential of L-Asparaginase isolated from Bacillus sp
Varying concentrations (31.25, 62.5, 125, 250, 500 μg/mL) of purified L-Asparaginase was tested on MCF7, HeLa, HepG2 and 3T3L1cell lines by MTT assay
Summary
Identification of the L-Asparaginase producing bacterial isolateL-asparaginase (L-asparagine amidohydrolase EC 3.5.1.1) is a hydrolase that plays a major role in the metabolism of all living organisms catalyzing the hydrolysis of L-asparagine to L-aspartic acid and ammonia (Lincoln and More, 2014). The enzyme is proven to have cytotoxic activity and is being used in the treatment of acute lymphoblastic leukemia. This is due to the fact that the leukemic cells do not have the property to produce L-asparagine, which is a nonessential amino acid, whereas the normal cells can produce their own. ELSPAR, ONCASPAR, ERWINASE and KIDROLASE are some of the brands of L-Asparaginase approved by FDA for the treatment of acute lymphoblastic leukemia and lymphosarcoma (Noura El-Ahmady et al, 2014) With reports suggesting difficulties in the bulk preparation of L-asparaginase from pig serum, focus has been shifted to alternate sources where sufficient amount of enzyme can be extracted (Verma et al, 2007). The objective of our research was to screen local soil and water isolates for L Asparaginase producers, purify and study the cytotoxic potential of the L-Asparaginase isolated
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