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Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose
BACKGROUND: Butanol is a second generation biofuel produced by Clostridium acetobutylicum through acetone-butanol-ethanol (ABE) fermentation process. Shotgun proteomics provides a direct approach to study the whole proteome of an organism in depth. This paper focuses on shotgun proteomic profiling o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3212805/ https://www.ncbi.nlm.nih.gov/pubmed/22008648 http://dx.doi.org/10.1186/1477-5956-9-66 |
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author | Sivagnanam, Kumaran Raghavan, Vijaya GS Shah, Manesh Hettich, Robert L Verberkmoes, Nathan C Lefsrud, Mark G |
author_facet | Sivagnanam, Kumaran Raghavan, Vijaya GS Shah, Manesh Hettich, Robert L Verberkmoes, Nathan C Lefsrud, Mark G |
author_sort | Sivagnanam, Kumaran |
collection | PubMed |
description | BACKGROUND: Butanol is a second generation biofuel produced by Clostridium acetobutylicum through acetone-butanol-ethanol (ABE) fermentation process. Shotgun proteomics provides a direct approach to study the whole proteome of an organism in depth. This paper focuses on shotgun proteomic profiling of C. acetobutylicum from ABE fermentation using glucose and xylose to understand the functional mechanisms of C. acetobutylicum proteins involved in butanol production. RESULTS: We identified 894 different proteins in C. acetobutylicum from ABE fermentation process by two dimensional - liquid chromatography - tandem mass spectrometry (2D-LC-MS/MS) method. This includes 717 proteins from glucose and 826 proteins from the xylose substrate. A total of 649 proteins were found to be common and 22 significantly differentially expressed proteins were identified between glucose and xylose substrates. CONCLUSION: Our results demonstrate that flagellar proteins are highly up-regulated with glucose compared to xylose substrate during ABE fermentation. Chemotactic activity was also found to be lost with the xylose substrate due to the absence of CheW and CheV proteins. This is the first report on the shotgun proteomic analysis of C. acetobutylicum ATCC 824 in ABE fermentation between glucose and xylose substrate from a single time data point and the number of proteins identified here is more than any other study performed on this organism up to this report. |
format | Online Article Text |
id | pubmed-3212805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-32128052011-11-11 Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose Sivagnanam, Kumaran Raghavan, Vijaya GS Shah, Manesh Hettich, Robert L Verberkmoes, Nathan C Lefsrud, Mark G Proteome Sci Research BACKGROUND: Butanol is a second generation biofuel produced by Clostridium acetobutylicum through acetone-butanol-ethanol (ABE) fermentation process. Shotgun proteomics provides a direct approach to study the whole proteome of an organism in depth. This paper focuses on shotgun proteomic profiling of C. acetobutylicum from ABE fermentation using glucose and xylose to understand the functional mechanisms of C. acetobutylicum proteins involved in butanol production. RESULTS: We identified 894 different proteins in C. acetobutylicum from ABE fermentation process by two dimensional - liquid chromatography - tandem mass spectrometry (2D-LC-MS/MS) method. This includes 717 proteins from glucose and 826 proteins from the xylose substrate. A total of 649 proteins were found to be common and 22 significantly differentially expressed proteins were identified between glucose and xylose substrates. CONCLUSION: Our results demonstrate that flagellar proteins are highly up-regulated with glucose compared to xylose substrate during ABE fermentation. Chemotactic activity was also found to be lost with the xylose substrate due to the absence of CheW and CheV proteins. This is the first report on the shotgun proteomic analysis of C. acetobutylicum ATCC 824 in ABE fermentation between glucose and xylose substrate from a single time data point and the number of proteins identified here is more than any other study performed on this organism up to this report. BioMed Central 2011-10-18 /pmc/articles/PMC3212805/ /pubmed/22008648 http://dx.doi.org/10.1186/1477-5956-9-66 Text en Copyright ©2011 Sivagnanam et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Sivagnanam, Kumaran Raghavan, Vijaya GS Shah, Manesh Hettich, Robert L Verberkmoes, Nathan C Lefsrud, Mark G Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose |
title | Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose |
title_full | Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose |
title_fullStr | Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose |
title_full_unstemmed | Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose |
title_short | Comparative shotgun proteomic analysis of Clostridium acetobutylicum from butanol fermentation using glucose and xylose |
title_sort | comparative shotgun proteomic analysis of clostridium acetobutylicum from butanol fermentation using glucose and xylose |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3212805/ https://www.ncbi.nlm.nih.gov/pubmed/22008648 http://dx.doi.org/10.1186/1477-5956-9-66 |
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