Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/2426
Title: Investigations on the bioproduction, purification and characterization of medicinally important L-asparaginase enzyme using a newly isolated bacterial species
Researcher: Madda, Sunitha
Guide(s): Ellaiah, P
Keywords: L-Asparaginase enzyme, Nutritional Parameters
Upload Date: 25-Aug-2011
University: Jawaharlal Nehru Technological University
Completed Date: August 2009
Abstract: A major potential therapeutic application of enzymes is in the treatment of cancer. Asparagianse has proved to be particularly promising for the treatment of acute lymphocytic leukaemia. Its action depends upon the fact that tumour cells are deficient in aspartate-ammonia ligase activity, which restricts their ability to synthesise the normally non-essential amino acid, L-asparagine. Therefore, they are forced to extract it from body fluids. The action of Asparaginase does not affect the functioning of normal cells, which are able to synthesise enough for their own requirements, but reduce the free exogenous concentration, and so induce a state of fatal starvation in the susceptible tumour cells. A 60% incidence of complete remission has been reported in a study of almost 6,000 cases of acute lymphocytic leukaemia. This enzyme is administered intravenously. MS-6 isolate was screened from different soil samples and taxonomic studies were also carried out. The selected promising isolate (MS-6)) was considered to be the novel strain of B. cereus and designated as B.cereus var. poluri for isolate MS-6. The different media tested, M-7 medium was found to be the best for L-asparaginase production (3.15 IU/mL). The optimal parameters are:, inoculum level of 10% v/v (3.15 IU/mL), age of inoculum 24 h (3.15 IU/mL), initial pH of 9.5 (4.23 IU/mL), incubation temperature of 28ºC (5.98 IU/mL), incubation period of 24 h (6.48 IU/mL), volume of 50 ml medium in 250 ml flask (7.86 IU/mL) and agitation speed of 120 rpm (8.16 IU/mL). The most effective mutagens, among UV mutants, MUV-9 showed the highest L-asparaginsase activity (24.98 IU/mL). it was 3.059 fold of the parent strain. The chemical mutagen (NTG) yielded a better enzyme producing mutant MNTG-7 with 38.06 IU/mL. newlineThus the strain improvement programme resulted in a mutant that produced 12.11 fold higher amount of the enzyme production over the parent wild strain (3.14 IU/mL), which is a very significant achievement in enzyme yield.
Pagination: 79p.
URI: http://hdl.handle.net/10603/2426
Appears in Departments:Faculty of Biotechnology

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01_title.pdfAttached File161.02 kBAdobe PDFView/Open
02_declaration.pdf58.17 kBAdobe PDFView/Open
03_certificate.pdf75.51 kBAdobe PDFView/Open
04_dedication.pdf51.05 kBAdobe PDFView/Open
05_abstract.pdf27 kBAdobe PDFView/Open
06_acknowledgements.pdf9.78 kBAdobe PDFView/Open
07_contents.pdf8.04 kBAdobe PDFView/Open
08_accronyms and abbreviations.pdf25.52 kBAdobe PDFView/Open
09_chapter 1.pdf503.3 kBAdobe PDFView/Open
10_chapter 2.pdf704.46 kBAdobe PDFView/Open
11_chapter 3.pdf312.8 kBAdobe PDFView/Open
12_chapter 4.pdf319.84 kBAdobe PDFView/Open
13_chapter 5.pdf926.89 kBAdobe PDFView/Open
14_chapter 6.pdf312.94 kBAdobe PDFView/Open
15_chapter 7.pdf518.16 kBAdobe PDFView/Open
16_chapter 8.pdf215.56 kBAdobe PDFView/Open
17_references.pdf149.5 kBAdobe PDFView/Open
18_appendix.pdf107.02 kBAdobe PDFView/Open
19_synopsyis.pdf171.33 kBAdobe PDFView/Open


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