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Proteome analysis of Acetobacter pasteurianus during acetic acid fermentation.
- Source :
-
Journal of proteomics [J Proteomics] 2012 Mar 16; Vol. 75 (6), pp. 1701-17. Date of Electronic Publication: 2011 Dec 02. - Publication Year :
- 2012
-
Abstract
- Acetic acid bacteria (AAB) are Gram-negative, strictly aerobic microorganisms that show a unique resistance to ethanol (EtOH) and acetic acid (AcH). Members of the Acetobacter and Gluconacetobacter genera are capable of transforming EtOH into AcH via the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes and are used for the industrial production of vinegar. Several mechanisms have been proposed to explain how AAB resist high concentrations of AcH, such as the assimilation of acetate through the tricarboxylic acid (TCA) cycle, the export of acetate by various transporters and modifications of the outer membrane. However, except for a few acetate-specific proteins, little is known about the global proteome responses to AcH. In this study, we used 2D-DIGE to compare the proteome of Acetobacter pasteurianus LMG 1262(T) when growing in glucose or ethanol and in the presence of acetic acid. Interesting protein spots were selected using the ANOVA p-value of 0.05 as threshold and 1.5-fold as the minimal level of differential expression, and a total of 53 proteins were successfully identified. Additionally, the size of AAB was reduced by approximately 30% in length as a consequence of the acidity. A modification in the membrane polysaccharides was also revealed by PATAg specific staining.<br /> (Copyright © 2011 Elsevier B.V. All rights reserved.)
- Subjects :
- Acetobacter genetics
Acetobacter ultrastructure
Culture Media metabolism
Ethanol metabolism
Fermentation
Glucose metabolism
Microscopy, Electron, Scanning
Protein Biosynthesis
Protein Folding
Tandem Mass Spectrometry
Two-Dimensional Difference Gel Electrophoresis
Up-Regulation
Acetic Acid metabolism
Acetobacter metabolism
Proteome metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1876-7737
- Volume :
- 75
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 22155126
- Full Text :
- https://doi.org/10.1016/j.jprot.2011.11.027