Data regarding the growth of  Lactobacillus acidophilus  NCFM on different carbohydrates and recombinant production of elongation factor G and pyruvate kinase

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Abstract

The present study describes the growth of the very well-known probiotic bacterium Lactobacillus acidophilus NCFM on different carbohydrates. Furthermore, recombinant production of putative moonlighting proteins elongation factor G and pyruvate kinase from this bacterium is described. For further and detailed interpretation of the data presented here, please see the research article “Mucin- and carbohydrate-stimulated adhesion and subproteome changes of the probiotic bacterium Lactobacillus acidophilus NCFM” (Celebioglu et al., 2017) [1].

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Most cited references 3

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Mucin- and carbohydrate-stimulated adhesion and subproteome changes of the probiotic bacterium Lactobacillus acidophilus NCFM.

Hasan Celebioglu, Sita Olesen, Kennie Prehn … (2017)

Adhesion to intestinal mucosa is a crucial property for probiotic bacteria. Adhesion is thought to increase host-bacterial interactions, thus potentially enabling health benefits to the host. Molecular events connected with adhesion and surface proteome changes were investigated for the probiotic Lactobacillus acidophilus NCFM cultured with established or emerging prebiotic carbohydrates as carbon source and in the presence of mucin, the glycoprotein of the epithelial mucus layer. Variation in adhesion to HT29-cells and mucin was associated with carbon source and mucin-induced subproteome abundancy differences. Specifically, while growth on fructooligosaccharides (FOS) only stimulated adhesion to intestinal HT-29 cells, cellobiose and polydextrose in addition increased adhesion to mucin. Adhesion to HT-29 cells increased by about 2-fold for bacteria grown on mucin-supplemented glucose. Comparative 2DE-MS surface proteome analysis showed different proteins in energy metabolism appearing on the surface, suggesting they exert moonlighting functions. Mucin-supplemented bacteria had relative abundance of pyruvate kinase and fructose-bisphosphate aldolase increased by about 2-fold while six spots with 3.2-2.1 fold reduced relative abundance comprised elongation factor G, phosphoglycerate kinase, BipAEFTU family GTP-binding protein, ribonucleoside triphosphate reductase, adenylosuccinate synthetase, 30S ribosomal protein S1, and manganese-dependent inorganic pyrophosphatase. Surface proteome of cellobiose- compared to glucose-grown L. acidophilus NCFM had phosphate starvation inducible protein stress-related, thermostable pullulanase, and elongation factor G increasing 4.4-2.4 fold, while GAPDH, elongation factor Ts, and pyruvate kinase were reduced by 2.0-1.5 fold in relative abundance. Addition of recombinant L. acidophilus NCFM elongation factor G and pyruvate kinase to a coated mucin layer significantly suppressed subsequent adhesion of the bacterium.

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Proteome reference map of Lactobacillus acidophilus NCFM and quantitative proteomics towards understanding the prebiotic action of lactitol.

Avishek Majumder, Abida Sultan, Rosa R Jersie-Christensen … (2011)

Lactobacillus acidophilus NCFM is a probiotic bacterium adapted to survive in the gastrointestinal tract and with potential health benefits to the host. Lactitol is a synthetic sugar alcohol used as a sugar replacement in low calorie foods and selectively stimulating growth of L. acidophilus NCFM. In the present study the whole-cell extract proteome of L. acidophilus NCFM grown on glucose until late exponential phase was resolved by 2-DE (pH 3-7). A total of 275 unique proteins assigned to various physiological processes were identified from 650 spots. Differential 2-DE (DIGE) (pH 4-7) of L. acidophilus NCFM grown on glucose and lactitol, revealed 68 spots with modified relative intensity. Thirty-two unique proteins were identified in 41 of these spots changing 1.6-12.7-fold in relative abundance by adaptation of L. acidophilus NCFM to growth on lactitol. These proteins included β-galactosidase small subunit, galactokinase, galactose-1-phosphate uridylyltransferase and UDP-glucose-4-epimerase, which all are potentially involved in lactitol metabolism. This first comprehensive proteome analysis of L. acidophilus NCFM provides insights into protein abundance changes elicited by the prebiotic lactitol. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Cloning, expression and characterization of a mucin-binding GAPDH from Lactobacillus acidophilus

Sarita Gupta, Desh Deepak Singh, Dhaval K Patel … (2016)

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Author and article information

Contributors

Birte Svensson

Journal

Journal ID (nlm-ta): Data Brief

Journal ID (iso-abbrev): Data Brief

Title: Data in Brief

Publisher: Elsevier

ISSN (Electronic): 2352-3409

Publication date PMC-release: 14 July 2017

Publication date Collection: October 2017

Publication date (Electronic): 14 July 2017

Volume: 14

Pages: 118-122

Affiliations

[a ]Enzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Denmark

[b ]Active Nutrition, DuPont, Nutrition & Health, Finland

[c ]Disease Systems Immunology, Department of Biotechnology and Biomedicine, Technical University of Denmark, Denmark

[d ]Protein Glycoscience and Biotechnology, Department of Biotechnology and Biomedicine, Technical University of Denmark, Denmark

Author notes

[* ]Corresponding author: Enzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Elektrovej, Building 375, DK-2800 Kgs. Lyngby, Denmark. Phone: +45 45252740. bis@ 123456bio.dtu.dk

Article

Publisher ID: S2352-3409(17)30323-2

DOI: 10.1016/j.dib.2017.07.021

PMC ID: 5567391

PubMed ID: 28861445

SO-VID: b0e4e2bf-9f60-4b2c-99cf-1f356db39a38

License:

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

History

Date received : 17 May 2017

Date accepted : 11 July 2017

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