Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/18663
Title: Engineering bacillus subtilis lipase for thermostability
Researcher: Acharya, Priyamvada
Guide(s): Rao, Madhusudan
Keywords: Cellular and molecular biology
Bacillus subtilis
Engineering bacillus
Tthermostability
Lipase
Guanidinium chloride
Upload Date: 26-May-2014
University: Jawaharlal Nehru University
Completed Date: 2002
Abstract: Structural solutions adapted by proteins to withstand changes in temp~rature newlinehave basic importance in the understanding of protein structure-function newlinerelations and also in industrial enzymology. Adaptability of protein structure is newlineexemplified by the discovery of enzymes that function at extremes of newlineenvironment. Proteins from extremophiles have become important in newlinedeciphering the strategies adapted by proteins to retain their functionalities in newlineextremes of environment. The conventional approach taken to understand newlinethermostability in proteins is to compare the structures of homologous proteins newlineisolated from thermophiles, mesophiles and psychrophiles. Such approaches newlinehave yielded insights into the importance of hydrophobicity, surface loops, salt newlinebridges, packing interactions etc. in protein thermostability. Given that the newlineenzymes have evolved over long periods during which thermal stress might not newlinehave been the only condition the protein had to adapt to, information gathered newlineby this approach is confounded by the plural effect of acquired mutations and newlineby the presence of mutations that are either silent or do not contribute to newlinethermostability. Despite several studies understanding the structural basis of newlinethermostability has proven elusive and till date, there are no well-defined rules newlineto stabilize a protein at high temperatures. Strategies that enable us to evolve newlineenzymes under defined conditions and controlled physical stresses can help newlineisolate protein variants with changes directly affecting the property of interest, newlinefor example, thermostability. These primary sequence variations can then be newlineprecisely mapped onto the structure. In vitro evolution is one such strategy, newlinewhich attempts to simulate the natural evolution in vitro in generation of variants newlineby error prone replicative processes and screening, for variants with the desired newlineproperty. newlineChapter 1 newlineGeneral aspects of protein thermostability and the structural features that newlinecontribute to protein thermostability are discussed.
Pagination: I,92p.
URI: http://hdl.handle.net/10603/18663
Appears in Departments:Centre for Cellular and Molecular Biology

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01_title.pdfAttached File11.39 kBAdobe PDFView/Open
02_certificate.pdf16.54 kBAdobe PDFView/Open
03_acknowledgements.pdf137.26 kBAdobe PDFView/Open
04_abbreviations.pdf23.13 kBAdobe PDFView/Open
05_contents.pdf77.43 kBAdobe PDFView/Open
06_abstract.pdf176.38 kBAdobe PDFView/Open
07_chapter 1.pdf1.11 MBAdobe PDFView/Open
08_chapter 2.pdf753.62 kBAdobe PDFView/Open
09_chapter 3.pdf2.95 MBAdobe PDFView/Open
10_chapter 4.pdf477.54 kBAdobe PDFView/Open
11_chapter 5.pdf928.32 kBAdobe PDFView/Open
12_chapter 6.pdf143.85 kBAdobe PDFView/Open
13_references.pdf135.31 kBAdobe PDFView/Open


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