Proteomic analysis reveals enzymes for β-D-glucan formation and degradation in Levilactobacillus brevis TMW 1.2112
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ABSTRACT: Bacterial exopolysaccharide (EPS) formation is crucial for biofilm formation, protection against environmental factors or as storage compounds. EPSs produced by lactic acid bacteria (LAB) are appropriate for applications in food fermentation or the pharmaceutical industry, yet the dynam-ics of formation and degradation thereof are rather poorly described. This study focuses on car-bohydrate active enzymes, including glycosyl transferases (GT) and glycoside hydrolases (GH), and their roles in the formation and potential degradation of O2-substituted (1,3)-β-D-glucan of Levilactobacillus (L.) brevis TMW 1.2112. The fermentation broth of L. brevis TMW 1.2112 was ana-lyzed for changes in viscosity, β-glucan and D-glucose concentrations during exponential, sta-tionary and early death phase. While the viscosity reached its maximum during stationary phase and subsequently decreased, the β-glucan concentration only increased to a plateau. Results were correlated with secretome and proteome data to identify involved enzymes and pathways. The suggested pathway for β-glucan biosynthesis involved a β-1,3 glucan synthase (GT2) and en-zymes from maltose phosphorylase (MP) operons. The decreased viscosity appeared to be associ-ated with cell lysis as the β-glucan concentration did not decrease most likely due to missing ex-tracellular carbohydrate active enzymes. In addition, an operon was discovered containing known moonlighting genes, all of which were detected in both proteome and secretome samples.
INSTRUMENT(S): Q Exactive HF-X
ORGANISM(S): Levilactobacillus Brevis
SUBMITTER: Christina Ludwig
LAB HEAD: Christina Ludwig
PROVIDER: PXD031809 | Pride | 2022-03-21
REPOSITORIES: Pride
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