Please use this identifier to cite or link to this item:
Title: Bioconversion of agricultural waste biomass for ethanol production
Researcher: Akhtar, Nadeem
Guide(s): Goyal, Dinesh
Keywords: Life Sciences,Microbiology,Biotechnology and Applied Microbiology
University: Thapar Institute of Engineering and Technology
Completed Date: 2014
Abstract: Conversion of lignocellulosic biomass to ethanol remains a key bottleneck at industrial scale to enhance the world energy security. Identification of promising feedstock, it s pre-treatment with process integration for enhanced saccharification by microbial conversion of substrate to ethanol is important in development sustainable energy system. Cellulose degrading bacteria from different sources such as compost, paper pulp and sugarcane bagasse were isolated, screened and characterized. Out of 32, eight bacterial isolates (designated as NA8, NA9, NA11, NA14, NA15, DGA, DGB and DGC) were found to be cellulose degraders. Biolog GEN III MicroPlateTM identification and 16S rRNA gene sequence analysis revealed that NA8, NA9, NA11, NA14, DGB and DGC showed maximum similarity with Bacillus licheniformis, isolate NA15 had maximum similarity with Bacillus subtilis whereas, DGA shared maximum similarity with Lysinibacillus fusiformis. Bacillus subtilis NA15 was found to be the best cellulose degrader among all the eight screened isolates with maximum carboxymethyl cellulase (CMCase) activity of 0.06 U/mL in cell free supernatant. Screening of 11 media ingredients using Plackett-Burman design was done to explicate the parameters that significantly influence the CMCase production. Maximum CMCase activity of 0.47 U/mL was obtained using Response surface methodology (RSM) with carboxy methyl cellulose (CMC): 18 g/L, peptone: 5 g/L, yeast extract: 5 g/L and MnCl2: 0.5 g/L. The model predicted the maximum CMCase activity (0.45U/mL) which was in good agreement with the experimental value of 0.47 U/mL showing 7-fold increase as compared to unoptimized medium. CMCase from Bacillus subtilis NA15 was purified using DEAE-Sepharose ion exchange chromatography with increase in CMCase activity from 2.65 to 30.42 U/mg of protein (11.5 fold) with a yield of 43.7%. The approximate molecular mass of the purified cellulase was 45 kDa.
Pagination: xxvii, 312p.
Appears in Departments:Department of Biotechnology

Files in This Item:
File Description SizeFormat 
file10(appendix and ra).pdfAttached File4.94 MBAdobe PDFView/Open
file1(title).pdf89.57 kBAdobe PDFView/Open
file2(certificate).pdf135.51 kBAdobe PDFView/Open
file3(preliminary pages).pdf646.1 kBAdobe PDFView/Open
file4(chapter 1).pdf170.86 kBAdobe PDFView/Open
file5(chapter 2).pdf1.63 MBAdobe PDFView/Open
file6(chapter 3).pdf1.61 MBAdobe PDFView/Open
file7(chapter 4.pdf3.76 MBAdobe PDFView/Open
file8(summary).pdf57.93 kBAdobe PDFView/Open
file9(references).pdf613.5 kBAdobe PDFView/Open

Items in Shodhganga are protected by copyright, with all rights reserved, unless otherwise indicated.