U.S. flag

An official website of the United States government

Dot gov

Official websites use .gov
A .gov website belongs to an official government organization in the United States.


Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.


Main content area

Proteomic analyses of ethanol tolerance in Lactobacillus buchneri NRRL B-30929

Siquing Liu
Proteomics 2014 v.14 no.21-22 pp. 2540-2544
Lactobacillus buchneri, amino acids, biocatalysts, carbohydrates, chaperonins, desorption, ethanol, ethanol fuels, ethanol production, fatty acid metabolism, fatty acids, fermentation, genetic engineering, growing media, lasers, mass spectrometry, membrane proteins, nitrogen, ornithine carbamoyltransferase, phenotype, phosphogluconate dehydrogenase, phosphoglycerate kinase, proteomics, redox potential, stress tolerance, transaminases, two-dimensional gel electrophoresis
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, Lbuc_1319) and phosphogluconate dehydrogenase (Lbuc_2157)]; nitrogen, amino acid and fatty acid metabolism [ureidoglycolate lyase (EC 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.