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Employing bacterial microcompartment technology to engineer a shell-free enzyme-aggregate for enhanced 1,2-propanediol production in Escherichia coli.

Lee, Matthew J., Brown, Ian R., Juodeikis, Rokas, Frank, Stefanie, Warren, Martin J. (2016) Employing bacterial microcompartment technology to engineer a shell-free enzyme-aggregate for enhanced 1,2-propanediol production in Escherichia coli. Metabolic Engineering, 36 . pp. 48-56. ISSN 1096-7176. (doi:10.1016/j.ymben.2016.02.007) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:54865)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://doi.org/10.1016/j.ymben.2016.02.007

Abstract

Bacterial microcompartments (BMCs) enhance the breakdown of metabolites such as 1,2-propanediol (1,2-PD) to propionic acid. The encapsulation of proteins within the BMC is mediated by the presence of targeting sequences. In an attempt to redesign the Pdu BMC into a 1,2-PD synthesising factory using glycerol as the starting material we added N-terminal targeting peptides to glycerol dehydrogenase, dihydroxyacetone kinase, methylglyoxal synthase and 1,2-propanediol oxidoreductase to allow their inclusion into an empty BMC. 1,2-PD producing strains containing the fused enzymes exhibit a 245% increase in product formation in comparison to un-tagged enzymes, irrespective of the presence of BMCs. Tagging of enzymes with targeting peptides results in the formation of dense protein aggregates within the cell that are shown by immuno-labelling to contain the vast majority of tagged proteins. It can therefore be concluded that these protein inclusions are metabolically active and facilitate the significant increase in product formation.

Item Type: Article
DOI/Identification number: 10.1016/j.ymben.2016.02.007
Uncontrolled keywords: Synthetic biology; Metabolic engineering; Compartmentalisation; Protein aggregation; Biotechnology;
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Susan Davies
Date Deposited: 11 Apr 2016 09:44 UTC
Last Modified: 23 Jan 2020 04:11 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/54865 (The current URI for this page, for reference purposes)
Warren, Martin J.: https://orcid.org/0000-0002-6028-6456
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