ArticleMicrobial cell factories2018
Production of the compatible solute α-D-glucosylglycerol by metabolically engineered Corynebacterium glutamicum.
Article in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 36 citations in OpenAlex.
- Photoautotrophic Production of 2-O-α-D-Glucosylglycerol by MarineMarine drugs · 2026Article
- α-glucosylglycerol: biological activities, emerging applications, and advances in sustainable biomanufacturing.World journal of microbiology & biotechnology · 2026Review
- Biocatalytic Production of 2-α-d-Glucosyl-glycerol for Functional Ingredient Use: Integrated Process Design and Techno-Economic Assessment.ACS sustainable chemistry & engineering · 2022Article
- Continuous process technology for glucoside production from sucrose using a whole cell-derived solid catalyst of sucrose phosphorylase.Applied microbiology and biotechnology · 2021Article
- Whole cell-based catalyst for enzymatic production of the osmolyte 2-O-α-glucosylglycerol.Microbial cell factories · 2021Article
- Salt-TolerantFrontiers in microbiology · 2021Article
- Exploring the Potential ofFrontiers in bioengineering and biotechnology · 2021Article
- The Industrial OrganismAntioxidants (Basel, Switzerland) · 2020Article
- Function of L-Pipecolic Acid as Compatible Solute inFrontiers in microbiology · 2019Article
- Salt-Regulated Accumulation of the Compatible Solutes Sucrose and Glucosylglycerol in Cyanobacteria and Its Biotechnological Potential.Frontiers in microbiology · 2019Review
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7 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundα-D-Glucosylglycerol (αGG) has beneficial functions as a moisturizing agent in cosmetics and potential as a health food material, and therapeutic agent. αGG serves as compatible solute in various halotolerant cyanobacteria such as Synechocystis sp. PCC 6803, which synthesizes αGG in a two-step reaction: The enzymatic condensation of ADP-glucose and glycerol 3-phosphate by GG-phosphate synthase (GGPS) is followed by the dephosphorylation of the intermediate by the GG-phosphate phosphatase (GGPP). The Gram-positive Corynebacterium glutamicum, an industrial workhorse for amino acid production, does not utilize αGG as a substrate and was therefore chosen for the development of a heterologous microbial production platform for αGG.
resultsPlasmid-bound expression of ggpS and ggpP from Synechocystis sp. PCC 6803 enabled αGG synthesis exclusively in osmotically stressed cells of C. glutamicum (pEKEx2-ggpSP), which is probably due to the unique intrinsic control mechanism of GGPS activity in response to intracellular ion concentrations. C. glutamicum was then engineered to optimize precursor supply for αGG production: The precursor for αGG synthesis ADP-glucose gets metabolized by both the glgA encoded glycogen synthase and the otsA encoded trehalose-6-phosphate synthase. Upon deletion of both genes the αGG concentration in culture supernatants was increased from 0.5 mM in C. glutamicum (pEKEx3-ggpSP) to 2.9 mM in C. glutamicum ΔotsA IMglgA (pEKEx3-ggpSP). Upon nitrogen limitation, which inhibits synthesis of amino acids as compatible solutes, C. glutamicum ΔotsA IMglgA (pEKEx3-ggpSP) produced more than 10 mM αGG (about 2 g L
conclusionsCorynebacterium glutamicum can be engineered as efficient platform for the production of the compatible solute αGG. Redirection of carbon flux towards αGG synthesis by elimination of the competing pathways for glycogen and trehalose synthesis as well as optimization of nitrogen supply is an efficient strategy to further optimize production of αGG.
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