Proteomic analyses of ethanol tolerance in Lactobacillus buchneri NRRL B-30929
2014
Liu, Siquing
The Lactobacillus buchneri NRRL B-30929 strain, isolated from a fuel ethanol production facility, exhibits high tolerance to environmental ethanol concentrations. This study aimed to identify proteins produced by B-30929 in response to environmental ethanol. Cellular proteins expressed by B-30929 growing in media with 10% vs. 0% ethanol were compared by 2D gel electrophoresis, followed by in gel digestion and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) analyses. Twenty ethanol responsive proteins were indentified. These include a proline-specific peptidase (Lbuc_1852); a membrane protein (Lbuc_0921), two general stress related 10 kDa chaperonin (GroESL Lbuc_1359) and a 29 kDa member of the HK 97 family (Lbuc_1523); metabolic enzymes involving redox potential balances (Lbuc_2051) and (Lbuc_0522)] and carbohydrate fermentation [phosphoglycerate kinase (EC 2.7.2.3, Lbuc_1319) and phosphogluconate dehydrogenase (Lbuc_2157)]; nitrogen, amino acid and fatty acid metabolism [ureidoglycolate lyase (EC 4.3.2.3 Lbuc_1994), ornithine carbamoyltransferase (Lbuc_0446), glycine hydroxymethytrasferase (Lbuc_0858), branched-chain amino acid aminotransferase Lbuc_0707), and fumarylacetoacetate hydrolase (Lbuc_0787)]. These changes suggested B-30929 cells respond to ethanol by degradation of available proteins and fatty acids and synthesis of new enzymes and molecular chaperons, plus a shift from oxidative to reductive metabolisms. These changes resulted in an ethanol-tolerant phenotype. These results can be used to guide genetic modifications to increase ethanol tolerance in industrial biocatalysts.
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