Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/2703
Title: Structural studies on phycocyanins from three cyanobacterial spp. and xylanase from an alkalophilic bacillus sp.
Researcher: Satyanarayana, L
Guide(s): Suresh, C G
Keywords: Biochemical Science
Upload Date: 9-Sep-2011
University: University of Pune
Completed Date: December 2006
Abstract: This thesis describes the research on C-phycocyanins (C-PC) from three cyanobacteria and an alkaline thermoactive xylanase (ATBXYL-C) from a Bacillus species. The first chapter involves a general introduction to the proteins under study, based on extensive review of available reports, publications and communications. The second chapter incorporates all the materials and methods employed in the course of the work. Next two chapters (3 & 4) record the results of various experiments on cyanobaterial phycocyanins, their analysis and comparison to existing knowledge. Similarly, last two chapters (5 & 6) involve documentation of results and relevant discussion about the xylanase. The major light-harvesting capacity of prokaryotic cyanobacteria and eukaryotic red algae is associated with large antennae complexes called phycobilisomes located on the surface of the photosynthetic thylakoid membranes. The phycobilisomes are composed of rods and a core, consisting of various phycobiliproteins and linker polypeptides. The phycobiliproteins are divided into three major classes: phycoerythrins, phycocyanins and allophycocyanins. The rods in phycobilisome normally have phycocyanin and the core has allophycocyanins. C-phycocyanins are composed of and subunits exhibiting high mutual affinity to form () monomers, which in turn aggregate into ()3 trimers and ()6 hexamers. Phycocyanins not only absorb light energy but also transfer the absorbed energy from phycoerythrins to allophycocyanins in the core and finally to the photosynthetic reaction center. In this thesis, we report the purification, crystallization and crystal structure analysis of C-PCs from the Indian cyanobacteria Phormidium and Lyngbya spp. Of marine habitat and Spirulina sp. of freshwater habitat. The crystal structure analysis of C-PCs has thrown light upon how the organization of C-PC units as seen in crystals helps in energy transfer. Xylanases produced by extremophiles are important due to their biotechnological applications and as model systems in structure-function studies. The paper and pulp industries use xylan-degrading enzymes for the pretreatment of paper pulp to enhance the bleaching effects. By using xylanases the quantity of bleaching chemicals can be reduced, thereby reducing the amount of toxic by-products and results in cost benefits also. Many studies on xylanases belonging to family G/11 have been reported.
Pagination: 253p.
URI: http://hdl.handle.net/10603/2703
Appears in Departments:Division of Biochemical Sciences, National Chemical Laboratory

Files in This Item:
File Description SizeFormat 
01_title.pdfAttached File226.36 kBAdobe PDFView/Open
02_declaration.pdf36.64 kBAdobe PDFView/Open
03_dedication.pdf34.28 kBAdobe PDFView/Open
04_acknowledgements.pdf49.17 kBAdobe PDFView/Open
05_contents.pdf84.05 kBAdobe PDFView/Open
06_abbreviations.pdf58.07 kBAdobe PDFView/Open
07_abstract.pdf95.97 kBAdobe PDFView/Open
08_chapter 1.pdf1.62 MBAdobe PDFView/Open
09_chapter 2.pdf218.47 kBAdobe PDFView/Open
10_chapter 3.pdf297.82 kBAdobe PDFView/Open
11_chapter 4.pdf4.09 MBAdobe PDFView/Open
12_chapter 5.pdf842.41 kBAdobe PDFView/Open
13_chapter 6.pdf2.82 MBAdobe PDFView/Open
14_references.pdf194.17 kBAdobe PDFView/Open


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