Cancer cells differentiate themselves from normal cells in diminished expression of L-asparaginase. It is the enzyme that catalyzes the hydrolysis of L-Asparagine to L-aspartic and ammonia, because of these it is used as a medication and in food manufacturing. As a medication L-aspraginase is used to treat various types of leukemia such as, acute lymphoblastic leukemia, acute myeloma leukemia and non Hodgkin’s lymphoma. Hence they are not capable of producing L-asparaginase and mainly depend on the L-asparagine from circulating plasma pools. The clinical action of this enzyme is attributed to the reduction of L-asparaginase, since tumor cells unable to synthesis these amino acids are selectively killed by L-asparaginase depravation. This enzyme is widely distributed, being found in as it is widely distributed bacteria as well as found in animals, microbes and plant sources. In the present study L-asparaginase producing bacteria was isolated from Simarouba glauca. It was grown on the modified M9 medium in which L- asparagine was the major source of L- asparaginase production was detected by the formation of pink colored zones on the medium. After the partial purification of the L-Asparaginase enzyme, the enzyme activity was found to be 155.83 Units/ml and specific activity of 779.15. The optimum pH was to be found at pH 8 at a temperature of 37°C in the presence of 10mM Mg2+. The molecular identification was done by16S rDNA, PCR and sequence analysis by BLAST further confirmed that Bacillus cereus.
| Published in | International Journal of Animal Science and Technology (Volume 3, Issue 1) |
| DOI | 10.11648/j.ijast.20190301.11 |
| Page(s) | 1-6 |
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This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
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Copyright © The Author(s), 2024. Published by Science Publishing Group |
L-Asparaginase, Simarouba Glauca, Bacillus Cereus, Enzyme Specific Activity, Cancer Cells
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APA Style
Pathuppilly Satheesan Kavya, Parakkottil Chothi Madhu. (2019). Isolation and Characterization of L- Asparaginase Producing Endophytic Bacteria from Simarouba Gluaca. International Journal of Animal Science and Technology, 3(1), 1-6. https://doi.org/10.11648/j.ijast.20190301.11
ACS Style
Pathuppilly Satheesan Kavya; Parakkottil Chothi Madhu. Isolation and Characterization of L- Asparaginase Producing Endophytic Bacteria from Simarouba Gluaca. Int. J. Anim. Sci. Technol. 2019, 3(1), 1-6. doi: 10.11648/j.ijast.20190301.11
AMA Style
Pathuppilly Satheesan Kavya, Parakkottil Chothi Madhu. Isolation and Characterization of L- Asparaginase Producing Endophytic Bacteria from Simarouba Gluaca. Int J Anim Sci Technol. 2019;3(1):1-6. doi: 10.11648/j.ijast.20190301.11
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Download@article{10.11648/j.ijast.20190301.11,
author = {Pathuppilly Satheesan Kavya and Parakkottil Chothi Madhu},
title = {Isolation and Characterization of L- Asparaginase Producing Endophytic Bacteria from Simarouba Gluaca},
journal = {International Journal of Animal Science and Technology},
volume = {3},
number = {1},
pages = {1-6},
doi = {10.11648/j.ijast.20190301.11},
url = {https://doi.org/10.11648/j.ijast.20190301.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijast.20190301.11},
abstract = {Cancer cells differentiate themselves from normal cells in diminished expression of L-asparaginase. It is the enzyme that catalyzes the hydrolysis of L-Asparagine to L-aspartic and ammonia, because of these it is used as a medication and in food manufacturing. As a medication L-aspraginase is used to treat various types of leukemia such as, acute lymphoblastic leukemia, acute myeloma leukemia and non Hodgkin’s lymphoma. Hence they are not capable of producing L-asparaginase and mainly depend on the L-asparagine from circulating plasma pools. The clinical action of this enzyme is attributed to the reduction of L-asparaginase, since tumor cells unable to synthesis these amino acids are selectively killed by L-asparaginase depravation. This enzyme is widely distributed, being found in as it is widely distributed bacteria as well as found in animals, microbes and plant sources. In the present study L-asparaginase producing bacteria was isolated from Simarouba glauca. It was grown on the modified M9 medium in which L- asparagine was the major source of L- asparaginase production was detected by the formation of pink colored zones on the medium. After the partial purification of the L-Asparaginase enzyme, the enzyme activity was found to be 155.83 Units/ml and specific activity of 779.15. The optimum pH was to be found at pH 8 at a temperature of 37°C in the presence of 10mM Mg2+. The molecular identification was done by16S rDNA, PCR and sequence analysis by BLAST further confirmed that Bacillus cereus.},
year = {2019}
}
TY - JOUR T1 - Isolation and Characterization of L- Asparaginase Producing Endophytic Bacteria from Simarouba Gluaca AU - Pathuppilly Satheesan Kavya AU - Parakkottil Chothi Madhu Y1 - 2019/02/07 PY - 2019 N1 - https://doi.org/10.11648/j.ijast.20190301.11 DO - 10.11648/j.ijast.20190301.11 T2 - International Journal of Animal Science and Technology JF - International Journal of Animal Science and Technology JO - International Journal of Animal Science and Technology SP - 1 EP - 6 PB - Science Publishing Group SN - 2640-1312 UR - https://doi.org/10.11648/j.ijast.20190301.11 AB - Cancer cells differentiate themselves from normal cells in diminished expression of L-asparaginase. It is the enzyme that catalyzes the hydrolysis of L-Asparagine to L-aspartic and ammonia, because of these it is used as a medication and in food manufacturing. As a medication L-aspraginase is used to treat various types of leukemia such as, acute lymphoblastic leukemia, acute myeloma leukemia and non Hodgkin’s lymphoma. Hence they are not capable of producing L-asparaginase and mainly depend on the L-asparagine from circulating plasma pools. The clinical action of this enzyme is attributed to the reduction of L-asparaginase, since tumor cells unable to synthesis these amino acids are selectively killed by L-asparaginase depravation. This enzyme is widely distributed, being found in as it is widely distributed bacteria as well as found in animals, microbes and plant sources. In the present study L-asparaginase producing bacteria was isolated from Simarouba glauca. It was grown on the modified M9 medium in which L- asparagine was the major source of L- asparaginase production was detected by the formation of pink colored zones on the medium. After the partial purification of the L-Asparaginase enzyme, the enzyme activity was found to be 155.83 Units/ml and specific activity of 779.15. The optimum pH was to be found at pH 8 at a temperature of 37°C in the presence of 10mM Mg2+. The molecular identification was done by16S rDNA, PCR and sequence analysis by BLAST further confirmed that Bacillus cereus. VL - 3 IS - 1 ER -
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