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Quantitative proteome profiles help reveal efficient xylose utilization mechanisms in solventogenic Clostridium sp. strain BOH3.

Authors :
Basu, Anindya
Xin, Fengxue
Lim, Teck Kwang
Lin, Qingsong
Yang, Kun‐Lin
He, Jianzhong
Source :
Biotechnology & Bioengineering; Sep2017, Vol. 114 Issue 9, p1959-1969, 11p
Publication Year :
2017

Abstract

ABSTRACT Development of sustainable biobutanol production platforms from lignocellulosic materials is impeded by inefficient five carbon sugar uptake by solventogenic bacteria. The recently isolated Clostridium sp. strain BOH3 is particularly advantaged in this regard as it serves as a model organism which can simultaneously utilize both glucose and xylose for high butanol (>15 g/L) production. Strain BOH3 was, therefore, investigated for its metabolic mechanisms for efficient five carbon sugar uptake using a quantitative proteomics based approach. The proteomics data show that proteins within the CAC1341-1349 operon play a pivotal role for efficient xylose uptake within the cells to produce butanol. Furthermore, up-regulation of key enzymes within the riboflavin synthesis pathway explained that xylose could induce higher riboflavin production capability of the bacteria (e.g., ∼80 mg/L from glucose vs. ∼120 mg/L from xylose). Overall results from the present experimental approach indicated that xylose-fed BOH3 cultures are subjected to high levels of redox stress which coupled with the solvent stress-trigger a sporulation response within the cells earlier than the glucose-fed cultures. The study lays the platform for metabolic engineering strategies in designing organisms for efficient butanol and other value-added chemicals such as riboflavin production. Biotechnol. Bioeng. 2017;114: 1959-1969. © 2017 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00063592
Volume :
114
Issue :
9
Database :
Complementary Index
Journal :
Biotechnology & Bioengineering
Publication Type :
Academic Journal
Accession number :
124256444
Full Text :
https://doi.org/10.1002/bit.26332