Anaerobic Reduction of Glycerol to Propanediol-1.3 by Lactobacillus brevis and Lactobacillus buchneri

Schütz, H.; Radler, F.

doi:10.1016/s0723-2020(84)80018-1

Cited by 171 publications

(83 citation statements)

References 18 publications

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“…A number of microorganisms have been shown to ferment glycerol in a 1,3-PDO-dependent manner, with the biological production of 1,3-PDO from glycerol demonstrated in Lactobacillus brevis, Lactobacillus buchnerii [21,22], Bacillus welchii [23], Citrobacter freundii, Klebsiella pneumoniae [24,25], Clostridium pasteurianum [26], and Clostridium butyricum [27][28][29]. 1,3-PDO is more reduced than glycerol resulting in glycerol fermentation producing 1,3-PDO and a more oxidized co-product.…”

Section: 3-propanediol (13-pdo)mentioning

confidence: 99%

Anaerobic fermentation of glycerol: a platform for renewable fuels and chemicals

Clomburg

González

2013

Trends in Biotechnology

271

184

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Section: 3-propanediol (13-pdo)mentioning

confidence: 99%

Anaerobic fermentation of glycerol: a platform for renewable fuels and chemicals

Clomburg

González

2013

Trends in Biotechnology

271

184

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“…The reduction of acrolein to allyl alcohol is especially intriguing, given the current interest in selective hydrogenation of acrolein to allyl alcohol in the chemical industry, where acrolein can be produced by selective dehydration of glycerol (Claus 1998;Gallezot and Richard 1998;Liu et al 2010). Acrolein can be metabolically produced from 3-HPA by spontaneous thermal intramolecular dehydration, a reaction that is enhanced at low pH (Schutz and Radler 1984). YqhD also has a low Km for malondialdehyde and could perform two reduction reactions on this substrate to produce 1,3-PD (Table 1).…”

Section: Unexplored Functionsmentioning

confidence: 99%

YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals

Jarboe

2010

Appl Microbiol Biotechnol

129

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The Escherichia coli NADPH-dependent aldehyde reductase YqhD has contributed to a variety of metabolic engineering projects for production of biorenewable fuels and chemicals. As a scavenger of toxic aldehydes produced by lipid peroxidation, YqhD has reductase activity for a broad range of short-chain aldehydes, including butyraldehyde, glyceraldehyde, malondialdehyde, isobutyraldehyde, methylglyoxal, propanealdehyde, acrolein, furfural, glyoxal, 3-hydroxypropionaldehyde, glycolaldehyde, acetaldehyde, and acetol. This reductase activity has proven useful for the production of biorenewable fuels and chemicals, such as isobutanol and 1,3-and 1,2-propanediol; additional capability exists for production of 1-butanol, 1-propanol, and allyl alcohol. A drawback of this reductase activity is the diversion of valuable NADPH away from biosynthesis. This YqhD-mediated NADPH depletion provides sufficient burden to contribute to growth inhibition by furfural and 5-hydroxymethyl furfural, inhibitory contaminants of biomass hydrolysate. The structure of YqhD has been characterized, with identification of a Zn atom in the active site. Directed engineering efforts have improved utilization of 3-hydroxypropionaldehyde and NADPH. Most recently, two independent projects have demonstrated regulation of yqhD by YqhC, where YqhC appears to function as an aldehyde sensor. AbstractThe Escherichia coli NADPH-dependent aldehyde reductase YqhD has contributed to a variety of metabolic engineering projects for production of biorenewable fuels and chemicals.As a scavenger of toxic aldehydes produced by lipid peroxidation, YqhD has reductase activity for a broad range of short-chain aldehydes, including butyraldehyde, glyceraldehyde, malondialdehyde, isobutyraldehyde, methylglyoxal, propanealdehyde, acrolein, furfural, glyoxal, 3-hydroxypropionaldehyde, glycolaldehyde, acetaldehyde and acetol. This reductase activity has proven useful for the production of biorenewable fuels and chemicals, such as isobutanol and 1,3-and 1,2-propanediol; additional capability exists for production of 1-butanol, 1-propanol and allyl alcohol. A drawback of this reductase activity is the diversion of valuable NADPH away from biosynthesis. This YqhD-mediated NADPH depletion provides sufficient burden to

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“…brevis and Lact. buchnerii (Schutz and Radler 1984) which use glycerol in cofermentation with sugars. Lactobacillus casei Cog 812 (Lonvaud-Funel 1986) uses glycerol as sole carbon source and glycerol kinase is the first enzyme involved.…”

Section: Introductionmentioning

confidence: 99%

Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p

Pasteris

Saad

1998

Lett Appl Microbiol

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S A AD . 1998. The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD-independent glycerol-3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28°C and pH 7·5 in 50 mmol l −1 TrisHCl buffer. The end-products of the reaction acted as competitive inhibitors while fructose-1,6-diphosphate was a non-competitive inhibitor. Mg 2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l −1 for glycerol and ATP, respectively. NAD-independent glycerol-3P dehydrogenase activity was maximal at 37°C and pH 7·5 in 100 mmol l −1 Tris-HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg 2+ and Ca 2+, but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non-competitive inhibitors.

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Anaerobic Reduction of Glycerol to Propanediol-1.3 by Lactobacillus brevis and Lactobacillus buchneri

Cited by 171 publications

References 18 publications

Anaerobic fermentation of glycerol: a platform for renewable fuels and chemicals

Anaerobic fermentation of glycerol: a platform for renewable fuels and chemicals

YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals

Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p

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