Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/33580
Title: Studies on production of protease and esterase from lysinibacillus fusiformisau01 purification biochemical characterization and application of protease
Researcher: Suryia prabham
Guide(s): Balasubramanian
Keywords: Central Composite Design
Response surface methodology
Upload Date: 5-Feb-2015
University: Anna University
Completed Date: 01/10/2014
Abstract: newlineProteases and Esterases are hydrolytic enzymes that catalyze the hydrolysis of peptide bonds and acylglycerols respectively Microbial proteases are currently receiving much attention because of their potential use in a variety of industries Shake flask cultures are widely used for studying the biotechnological process due to minimal cost of materials and ease of maintenance Optimization of media components by methods which involves the change of one variable at a time was extremely time consuming and expensive when a large number of variables were considered In order to overcome this difficulty and determine the interaction between the studied variables an experimental factorial design and response surface methodology RSM was employed for the optimization process In this work we report the finding of production of protease and esterase purification biochemical characterisation and application of protease enzyme from Lysinibacillus fusiformisAU01 The optimum media components and physical factors for protease and esterase secretion and production were investigated by one variable at a time approach followed by Plackett Burman design and further optimized by Central Composite Design CCD and Response Surface Methodology RSM fullfactorial design Nine variables such as as trisodium citrate yeast extract CaCl2 MgSO4 pH newlineinoculum size Temperature Incubation time and agitation affecting protease production were identified by one factor at a time approach their effects were evaluated using Plackett Burman design newline
Pagination: xx, 118p.
URI: http://hdl.handle.net/10603/33580
Appears in Departments:Faculty of Science and Humanities

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03_abstract.pdf17.53 kBAdobe PDFView/Open
04_acknowledgement.pdf6.68 kBAdobe PDFView/Open
05_content.pdf35.4 kBAdobe PDFView/Open
06_chapter1.pdf484.41 kBAdobe PDFView/Open
07_chapter2.pdf197.15 kBAdobe PDFView/Open
08_chapter3.pdf2.62 MBAdobe PDFView/Open
09_chapter4.pdf15.84 kBAdobe PDFView/Open
10_appendix.pdf49.19 kBAdobe PDFView/Open
11_reference.pdf297.13 kBAdobe PDFView/Open
12_publication.pdf10.2 kBAdobe PDFView/Open
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