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Title: Characterization and Immobilization studies on nitrilase enzyme of Rhodococcus pyridinivorans NIT 36
Researcher: Jyoti
Guide(s): Seth Amit
Keywords: Life Sciences,Microbiology,Biotechnology and Applied Microbiology
University: Shoolini University of Biotechnology and Management Sciences
Completed Date: 31-01-2018
Abstract: newline x newlineABSTRACT newlineThe aim of present study was optimizing the reaction parameters, immobilization, amplification, cloning and molecular homology and docking. Maximum activity observed at temperature 40°C and pH 7.5 for free cells and for immobilized cells temperature observed was 60°C and pH 7.0. Microbial isolate NIT-36 was showed maximum nitrilase activity in 150 mM concentration of substrate (benzonitrile) for free cells and 200 mM substrate (acrylonitrile) concentration for immobilized cells. newlineUsing RSM, it was possible to model the crucial factors and their interactive effects on production of nitrilase. The statistical analysis revealed that the immobilized nitrilase was stable even at temperatures exceeding 50ºC and was capable of effectively biotransforming higher levels of substrate into its corresponding product. A 2.38 fold enhancement in nitrilase activity for non-immobilized cells and a 4.39 fold improvement in the nitrilase activity of immobilized cells underline the utility of employing a statistical optimization approach. newlinePCR based tools were utilized to identify the genes responsible for nitrilase activity of Rhodococcus pyridinivornas NIT-36. The changes at the protein level were also recorded by using various bioinformatics tools. We were able found the composition of nitrilase protein of R. pyridinivorans NIT-36. This was assisted by carrying out different docking studies which ultimately resulted in gaining a superior insight into the functioning of the nitrilase enzyme.
Pagination: 142
Appears in Departments:Faculty Of Biotechnology

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10. list of figures.pdfAttached File115 kBAdobe PDFView/Open
11. abstract.pdf81.9 kBAdobe PDFView/Open
12. introduction.pdf250.97 kBAdobe PDFView/Open
13. review.pdf887.03 kBAdobe PDFView/Open
14. material and methods.pdf474.1 kBAdobe PDFView/Open
15. results.pdf4.15 MBAdobe PDFView/Open
16. discussion.pdf305 kBAdobe PDFView/Open
17. summary and conclusion.pdf161.1 kBAdobe PDFView/Open
18. future directions.pdf80.91 kBAdobe PDFView/Open
19. references.pdf436.23 kBAdobe PDFView/Open
1. title page.pdf196.95 kBAdobe PDFView/Open
20. appendix.pdf650.38 kBAdobe PDFView/Open
21. publications.pdf239.2 kBAdobe PDFView/Open
2. declaration by the candidate.pdf124.24 kBAdobe PDFView/Open
3. certificate 1.pdf129.98 kBAdobe PDFView/Open
4. certificate 2.pdf122.31 kBAdobe PDFView/Open
5. certificate 3.pdf249.23 kBAdobe PDFView/Open
6. contents.pdf328.01 kBAdobe PDFView/Open
7. acknowledgement.pdf115.54 kBAdobe PDFView/Open
8. list of symbols and abbreviations.pdf97.18 kBAdobe PDFView/Open
9. table list.pdf89.1 kBAdobe PDFView/Open
paper-1.pdf338.47 kBAdobe PDFView/Open
paper-2.pdf1.61 MBAdobe PDFView/Open
paper-3.pdf3.77 MBAdobe PDFView/Open

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