There is huge variability among yeasts with regard to their efficiency in utilizing glycerol as the sole source of carbon and energy. Certain species show growth rates with glycerol comparable to those reached with glucose as carbon source; others are virtually unable to utilize glycerol, especially in synthetic medium. Most of our current knowledge regarding glycerol uptake and its catabolic pathways has been gained from studying laboratory strains of the model yeast Saccharomyces cerevisiae. The growth of these strains on glycerol is dependent on the presence of medium supplements such as amino acids and nucleobases. In contrast, there is only fragmentary knowledge about S. cerevisiae isolates able to grow in synthetic glycerol medium without such supplements as well as about growth of non-Saccharomyces yeast species on glycerol. Thus, more research is required to understand why certain strains and species show superior growth performance on glycerol compared to common S. cerevisiae laboratory strains. This minireview summarizes what is known so far about the gene products and pathways involved in glycerol metabolism and transport in yeast and fungi as well as the regulation of these processes. This article is protected by copyright. All rights reserved.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/1462-2920.13617

Glycerol metabolism and transport in yeast and fungi: established knowledge and ambiguities.

The functional reconstruction of acetoin and meso-2,3-butanediol (meso-2,3-BD) biosynthetic pathways in Escherichia coli have been explored systematically. Pathway construction involved the in vsivo screening of prospective pathway isozymes of yeast and bacterial origin. After substantial engineering of the host background to increase pyruvate availability, E. coli YYC202(DE3) ldhA(ilvC( expressing ilvBN from E. coli and aldB from L. lactis (encoding acetolactate synthase and acetolactate decarboxylase activities, respectively) was able to produce up to 870 mg/L acetoin, with no coproduction of diacetyl observed. These strains were also found to produce small quantities of meso-2,3-BD, suggesting the existence of endogenous 2,3-BD dehydrogenase activity. Finally, the coexpression of bdh1 from S. cerevisiae, encoding 2,3-BD dehydrogenase, in this strain resulted in the production of up to 1120 mg/L meso-2,3-BD, with glucose a yield of 0.29 g/g. While disruption of the native lactate biosynthesis pathway increased pyruvate precursor availability to this strain, increased availability of NADH for acetoin reduction to meso-2,3-BD was found to be the most important consequence of ldhA deletion.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.200900279

Metabolic engineering of acetoin and meso-2, 3-butanediol biosynthesis in E. coli.

Background
2,3-Butanediol (2,3-BD), a platform and fuel bio-chemical, can be efficiently produced by Klebsiella pneumonia, K. oxytoca, and Serratia marcescens. However, these strains are opportunistic pathogens and not favorable for industrial application. Although some generally regarded as safe (GRAS) microorganisms have been isolated in recent years, there is still a demand for safe 2,3-BD producing strains with high productivity and yield under thermophilic fermentation.

/pdf/a-newly-isolated-bacillus-licheniformis-strain-1r2hoqhrom.pdf

A newly isolated Bacillus licheniformis strain thermophilically produces 2,3-butanediol, a platform and fuel bio-chemical

2,3-Butanediol (2,3-BD) can be used as a liquid fuel additive to replace petroleum oil, and as an important platform chemical in the pharmaceutical and plastic industries. Microbial production of 2,3-BD by Bacillus licheniformis presents potential advantages due to its GRAS status, but previous attempts to use this microorganism as a chassis strain resulted in the production of a mix of D-2,3-BD and meso-2,3-BD isomers. The aim of this work was to develop an engineered strain of B. licheniformis suited to produce the high titers of the pure meso-2,3-BD isomer. Glycerol dehydrogenase (Gdh) was identified as the catalyst for D-2,3-BD biosynthesis from its precursor acetoin in B. licheniformis. The gdh gene was, therefore, deleted from the wild-type strain WX-02 to inhibit the flux of acetoin to D-2,3-BD biosynthesis. The acoR gene involved in acetoin degradation through AoDH ES was also deleted to provide adequate flux from acetoin towards meso-2,3-BD. By re-directing the carbon flux distribution, the double-deletion mutant WX-02ΔgdhΔacoR produced 28.2 g/L of meso-2,3-BD isomer with >99 % purity. The titer was 50 % higher than that of the wide type. A bench-scale fermentation by the double-deletion mutant was developed to further improve meso-2,3-BD production. In a fed-batch fermentation, meso-2,3-BD titer reached 98.0 g/L with a purity of >99.0 % and a productivity of 0.94 g/L–h. This work demonstrates the potential of producing meso-2,3-BD with high titer and purity through metabolic engineering of B. licheniformis.

/pdf/engineering-bacillus-licheniformis-for-the-production-of-2pw8s7e0ec.pdf

Engineering Bacillus licheniformis for the production of meso-2,3-butanediol

Homologous overexpression of hydrogenase and glycerol dehydrogenase in Clostridium pasteurianum to enhance hydrogen production from crude glycerol

Glycerol dehydrogenase (EC 1.1.1.6) was purified from a methylotrophic yeast, Hansenula polymorpha DL-1, for the characterisation and identification of its function. The yeast was grown in a glycerol medium. SDS-PAGE and gel permeation chromatography showed the enzyme to be composed of two subunits, each with a molecular mass of 36,000. The optimum pH for glycerol oxidation was 10. The optimum temperature for enzyme activity was 30 °C. CuCl 2 , HgCl 2 , and FeCl 3 were severely inhibitory. The activity decreased to 0% by 1 mM 2, 2'-dipyridyl and o-phenanthroline, which are inhibitors for the Fe 2+ -enzyme. An SH reagent, p-chloromercuribenzoate, was strongly inhibitory at 0.1 mM. The enzyme showed greater activity towards (R)-1,2-propanediol and (2R,3R)-2,3-butanediol than towards glycerol. No activity was detected towards 1.3-propanediol, ethanol, 1-propanol, 2-propanol, propionic acid, 1,4-butanediol, 1,2,3,4-butanetetraol, sorbitol, and L-iditol. The ratios of the activity for the R-form to that of the S-form were 5.0(R): 1(S) and 38 (R): 1(S) for 1,2-propanediol and 2,3-butanediol, respectively. The K m values for glycerol and dihydroxyacetone were 118 mM and 4.87 μM, respectively. The gene encoding the enzyme was cloned from an H. polymorpha DL-1 genomic library. Reverse transcription PCR showed that the mRNA of the enzyme was synthesised in cells grown on methanol as well as on glycerol. In the deduced amino acid sequence of 380 residues of the glycerol dehydrogenase of H. polymorpha DL-1, the NAD(H) binding pattern and the cysteine residues that correspond to the cysteine ligands at the zinc atom were conserved, as they are in sorbitol dehydrogenase, L-iditol 2-dehydrogenase, and 2,3-butanediol dehydrogenase from other origins.

Characterisation of Glycerol Dehydrogenase from a Methylotrophic Yeast, Hansenula polymorpha Dl‐1, and its Gene Cloning

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Characterisation of Glycerol Dehydrogenase from a Methylotrophic Yeast, Hansenula polymorpha Dl‐1, and its Gene Cloning