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Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose.
J Biotechnol. 2014 Nov 10; 189:27-35.JB

Abstract

Gluconobacter strains are specialized in the incomplete oxidation of monosaccharides. In contrast, growth and product formation from disaccharides is either very low or impossible. A pathway that allows growth on trehalose was rationally designed to broaden the substrate range of Gluconobacter oxydans. Expression vectors containing different signal sequences and the gene encoding alkaline phosphatase, phoA, from Escherichia coli were constructed. The signal peptide that exhibited the strongest periplasmic PhoA activity was used to generate a G. oxydans strain able to utilize the model disaccharide trehalose as a carbon and energy source by expressing the periplasmic trehalase TreA from E. coli. The strain had a doubling time of 3.7h and reached a final optical density of 1.7 when trehalose was used as a growth substrate. In comparison, the wild-type harboring the empty vector and the strain expressing treA without a signal sequence grew slowly to a final OD of only 0.15. The trehalose concentration in treA expressing cultures decreased continuously during the exponential growth phase indicating that the substrate was hydrolyzed to glucose by TreA. In contrast to the wild-type growing on glucose, the treA expression strain mainly formed acetate and 5-ketogluconate as end products rather than gluconate.

Authors+Show Affiliations

Institute of Microbiology and Biotechnology, University of Bonn, 168 Meckenheimer Allee, 53115 Bonn, Germany.Institute of Microbiology and Biotechnology, University of Bonn, 168 Meckenheimer Allee, 53115 Bonn, Germany.Missouri State University, Biology Department, 901 S. National Avenue, Springfield, MO 65897, United States.Institute of Microbiology and Biotechnology, University of Bonn, 168 Meckenheimer Allee, 53115 Bonn, Germany. Electronic address: udeppen@uni-bonn.de.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25179874

Citation

Kosciow, K, et al. "Production of a Periplasmic Trehalase in Gluconobacter Oxydans and Growth On Trehalose." Journal of Biotechnology, vol. 189, 2014, pp. 27-35.
Kosciow K, Zahid N, Schweiger P, et al. Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose. J Biotechnol. 2014;189:27-35.
Kosciow, K., Zahid, N., Schweiger, P., & Deppenmeier, U. (2014). Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose. Journal of Biotechnology, 189, 27-35. https://doi.org/10.1016/j.jbiotec.2014.08.029
Kosciow K, et al. Production of a Periplasmic Trehalase in Gluconobacter Oxydans and Growth On Trehalose. J Biotechnol. 2014 Nov 10;189:27-35. PubMed PMID: 25179874.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose. AU - Kosciow,K, AU - Zahid,N, AU - Schweiger,P, AU - Deppenmeier,U, Y1 - 2014/08/30/ PY - 2014/07/07/received PY - 2014/08/19/revised PY - 2014/08/21/accepted PY - 2014/9/3/entrez PY - 2014/9/3/pubmed PY - 2015/8/27/medline KW - Acetic acid bacteria KW - Genetic tool KW - Incomplete oxidation KW - Signal peptide KW - Substrate spectrum SP - 27 EP - 35 JF - Journal of biotechnology JO - J Biotechnol VL - 189 N2 - Gluconobacter strains are specialized in the incomplete oxidation of monosaccharides. In contrast, growth and product formation from disaccharides is either very low or impossible. A pathway that allows growth on trehalose was rationally designed to broaden the substrate range of Gluconobacter oxydans. Expression vectors containing different signal sequences and the gene encoding alkaline phosphatase, phoA, from Escherichia coli were constructed. The signal peptide that exhibited the strongest periplasmic PhoA activity was used to generate a G. oxydans strain able to utilize the model disaccharide trehalose as a carbon and energy source by expressing the periplasmic trehalase TreA from E. coli. The strain had a doubling time of 3.7h and reached a final optical density of 1.7 when trehalose was used as a growth substrate. In comparison, the wild-type harboring the empty vector and the strain expressing treA without a signal sequence grew slowly to a final OD of only 0.15. The trehalose concentration in treA expressing cultures decreased continuously during the exponential growth phase indicating that the substrate was hydrolyzed to glucose by TreA. In contrast to the wild-type growing on glucose, the treA expression strain mainly formed acetate and 5-ketogluconate as end products rather than gluconate. SN - 1873-4863 UR - https://www.unboundmedicine.com/medline/citation/25179874/Production_of_a_periplasmic_trehalase_in_Gluconobacter_oxydans_and_growth_on_trehalose_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0168-1656(14)00834-7 DB - PRIME DP - Unbound Medicine ER -