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Overproduction of trehalose: heterologous expression of Escherichia coli trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase in Corynebacterium glutamicum.
Appl Environ Microbiol. 2004 Jan; 70(1):370-6.AE

Abstract

Trehalose is a disaccharide with potential applications in the biotechnology and food industries. We propose a method for industrial production of trehalose, based on improved strains of Corynebacterium glutamicum. This paper describes the heterologous expression of Escherichia coli trehalose-synthesizing enzymes trehalose-6-phosphate synthase (OtsA) and trehalose-6-phosphate phosphatase (OtsB) in C. glutamicum, as well as its impact on the trehalose biosynthetic rate and metabolic-flux distributions, during growth in a defined culture medium. The new recombinant strain showed a five- to sixfold increase in the activity of OtsAB pathway enzymes, compared to a control strain, as well as an almost fourfold increase in the trehalose excretion rate during the exponential growth phase and a twofold increase in the final titer of trehalose. The heterologous expression described resulted in a reduced specific glucose uptake rate and Krebs cycle flux, as well as reduced pentose pathway flux, a consequence of downregulated glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. The results proved the suitability of using the heterologous expression of Ots proteins in C. glutamicum to increase the trehalose biosynthetic rate and yield and suggest critical points for further improvement of trehalose overproduction in C. glutamicum.

Authors+Show Affiliations

Departmento de Ingeniería Química y Bioprocesos, Escuela de Ingeniería, Pontificia Universidad Católica de Chile, Santiago, Chile.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

14711665

Citation

Padilla, Leandro, et al. "Overproduction of Trehalose: Heterologous Expression of Escherichia Coli Trehalose-6-phosphate Synthase and Trehalose-6-phosphate Phosphatase in Corynebacterium Glutamicum." Applied and Environmental Microbiology, vol. 70, no. 1, 2004, pp. 370-6.
Padilla L, Krämer R, Stephanopoulos G, et al. Overproduction of trehalose: heterologous expression of Escherichia coli trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase in Corynebacterium glutamicum. Appl Environ Microbiol. 2004;70(1):370-6.
Padilla, L., Krämer, R., Stephanopoulos, G., & Agosin, E. (2004). Overproduction of trehalose: heterologous expression of Escherichia coli trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase in Corynebacterium glutamicum. Applied and Environmental Microbiology, 70(1), 370-6.
Padilla L, et al. Overproduction of Trehalose: Heterologous Expression of Escherichia Coli Trehalose-6-phosphate Synthase and Trehalose-6-phosphate Phosphatase in Corynebacterium Glutamicum. Appl Environ Microbiol. 2004;70(1):370-6. PubMed PMID: 14711665.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Overproduction of trehalose: heterologous expression of Escherichia coli trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase in Corynebacterium glutamicum. AU - Padilla,Leandro, AU - Krämer,Reinhard, AU - Stephanopoulos,Gregory, AU - Agosin,Eduardo, PY - 2004/1/9/pubmed PY - 2004/4/9/medline PY - 2004/1/9/entrez SP - 370 EP - 6 JF - Applied and environmental microbiology JO - Appl Environ Microbiol VL - 70 IS - 1 N2 - Trehalose is a disaccharide with potential applications in the biotechnology and food industries. We propose a method for industrial production of trehalose, based on improved strains of Corynebacterium glutamicum. This paper describes the heterologous expression of Escherichia coli trehalose-synthesizing enzymes trehalose-6-phosphate synthase (OtsA) and trehalose-6-phosphate phosphatase (OtsB) in C. glutamicum, as well as its impact on the trehalose biosynthetic rate and metabolic-flux distributions, during growth in a defined culture medium. The new recombinant strain showed a five- to sixfold increase in the activity of OtsAB pathway enzymes, compared to a control strain, as well as an almost fourfold increase in the trehalose excretion rate during the exponential growth phase and a twofold increase in the final titer of trehalose. The heterologous expression described resulted in a reduced specific glucose uptake rate and Krebs cycle flux, as well as reduced pentose pathway flux, a consequence of downregulated glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. The results proved the suitability of using the heterologous expression of Ots proteins in C. glutamicum to increase the trehalose biosynthetic rate and yield and suggest critical points for further improvement of trehalose overproduction in C. glutamicum. SN - 0099-2240 UR - https://www.unboundmedicine.com/medline/citation/14711665/Overproduction_of_trehalose:_heterologous_expression_of_Escherichia_coli_trehalose_6_phosphate_synthase_and_trehalose_6_phosphate_phosphatase_in_Corynebacterium_glutamicum_ L2 - https://journals.asm.org/doi/10.1128/AEM.70.1.370-376.2004?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -