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 |
| Creative Commons |
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), 2019. Published by Science Publishing Group |
L-Asparaginase, Simarouba Glauca, Bacillus Cereus, Enzyme Specific Activity, Cancer Cells
| [1] | Savitri, Neeta Asthanan and Wamik Azmi (2002). Microbial L-asparginase: a potent antitumor enzyme Indian journal of Biotechnology Vol:2 pp 184 -194. |
| [2] | Joshi S R, and Fenella M War Nongkhlaw (2015). L-aspargnese and antioxidant activity endophytic associated bacteria with ethanomedical plants, Indian journal of Biotechnology pp 59 – 64. |
| [3] | Buchanan. R. G and Gibbons. N. E. (1975) Bergey’s Manual of Determinative Bacteriology 8th ed., Williams and Wikins Baltimore Inc Baltimore 2 md USA. |
| [4] | Lowry O H, Rosebrough N J, Farr A L, Randall R J. (1951). Protein measurement with the Folin phenol reagent. Biol Chem. (1):265-75. |
| [5] | Salini Dinesh, Devi Soorya Narayana Sasikumar, Bala Girija, Lakshmipriya V. Panicker, Pooja Vinod Kumar, Sruthy Preetha, Shaima Santhilal Sarma (2017) Pharmacological evaluation of endophytic Penicillium pimiteouiense SGS isolated from Simarouba glauca DC, Journal of Applied Pharmaceutical Science Vol. 7 (09), pp. 142-147. |
| [6] | John C. Wriston, AsparaginaseMethods in Enzymology. (1970). Volume 17, Part A, Pages 732-742. |
| [7] | Gulati R, Tsodikov A, Etzioni R, Hunter-Merrill RA, Gore JL, Mariotto AB, Cooperberg MR (2014) Expected population impacts of discontinued prostate-specific antigen screening, Cancer. 15;120 (22):3519-26. |
| [8] | Mohapatra, B. R. & Sani, Khairul & Banerjee, U. C. (2008). Characterization of L‐asparaginase from Bacillus sp. isolated from an intertidal marine alga (Sargassum sp.). Letters in Applied Microbiology. 21. 380 - 383. 10.1111. |
| [9] | Arif, H M Hussain Z (2014) important sources and medical applications of L-aspargenase. Int J Pharm Sci Rev, 3 35-45. |
| [10] | Noura El-Ahmady El-Naggar, Sahar F. Deraz, Hoda M. Soliman, Nehal M. El-Deeb, Sara M. El-Ewasy. Purification, characterization, cytotoxicity and anticancer activities of L-asparaginase, anti-colon cancer protein, from the newly isolated alkaliphilic Streptomyces fradiae NEAE-82 BMC Pharmacology and Toxicology Sept 2016. |
| [11] | Gulati R, Saxena R K, Gupta R. A (1997). Rapid plate assay for screening L-asparaginase producing micro-organisms. Lett Appl Microbiol. 24(1):23-6. |
| [12] | Zahid H, Ali H, Soudan H, Embaby A, Farag A, Hussein A, Ataya F (2018). Molecular cloning, structural modeling and production of recombinant Aspergillus terreusl. asparaginase in Escherichia coli. Int. J. Biol. Macromol. Jan; pp 1041-1051. |
| [13] | Renuka D Joshi, Nikhilesh S Kulkarni (2006). Optimization studies on L-asparaginase production from endophytic Bacteria, International Journal of Applied Research 2016; 2(3): 624-629. |
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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