Widespread distribution of hmf genes in Proteobacteria reveals key enzymes for 5-hydroxymethylfurfural conversion

Donoso, Raúl; González-Toro, F.; Pérez‐Pantoja, Danilo

doi:10.1016/j.csbj.2021.04.017

Cited by 11 publications

(4 citation statements)

References 69 publications

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“…Bacteria and plasmids used in this study are listed in Table 1 . Rhodococcus species and Cupriavidus pinatubonensis JMP134 derivatives were grown at 30 °C in mineral salts medium previously reported [ 29 ], supplemented with 5 mM VA, PCA, 3-methoxybenzoate (3-MB), 5-methoxysalicylate (5-MS), gentisate, 3-hydroxybenzoate (3-HB), 3-methoxyphenylacetate, 3-hydroxyphenylacetate, 3-methoxysalicylate, 2,3-dihydroxybenzoate, syringate and homovanillate, as sole carbon and energy source. Escherichia coli Mach1 (Invitrogen, Carlsbad, CA, USA) was grown at 37 °C in Luria-Bertani (LB) medium.…”

Section: Methodsmentioning

confidence: 99%

Identification of a Phylogenetically Divergent Vanillate O-Demethylase from Rhodococcus ruber R1 Supporting Growth on Meta-Methoxylated Aromatic Acids

et al. 2022

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Rieske-type two-component vanillate O-demethylases (VanODs) catalyze conversion of the lignin-derived monomer vanillate into protocatechuate in several bacterial species. Currently, VanODs have received attention because of the demand of effective lignin valorization technologies, since these enzymes own the potential to catalyze methoxy group demethylation of distinct lignin monomers. In this work, we identified a phylogenetically divergent VanOD from Rhodococcus ruber R1, only distantly related to previously described homologues and whose presence, along with a 3-hydroxybenzoate/gentisate pathway, correlated with the ability to grow on other meta-methoxylated aromatics, such as 3-methoxybenzoate and 5-methoxysalicylate. The complementation of catabolic abilities by heterologous expression in a host strain unable to grow on vanillate, and subsequent resting cell assays, suggest that the vanAB genes of R1 strain encode a proficient VanOD acting on different vanillate-like substrates; and also revealed that a methoxy group in the meta position and a carboxylic acid moiety in the aromatic ring are key for substrate recognition. Phylogenetic analysis of the oxygenase subunit of bacterial VanODs revealed three divergent groups constituted by homologues found in Proteobacteria (Type I), Actinobacteria (Type II), or Proteobacteria/Actinobacteria (Type III) in which the R1 VanOD is placed. These results suggest that VanOD from R1 strain, and its type III homologues, expand the range of methoxylated aromatics used as substrates by bacteria.

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Section: Methodsmentioning

confidence: 99%

Identification of a Phylogenetically Divergent Vanillate O-Demethylase from Rhodococcus ruber R1 Supporting Growth on Meta-Methoxylated Aromatic Acids

et al. 2022

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“…One of the main disadvantages of the latter is the formation of microbial growth inhibitors, furfural (FF), 5-Hydroxymethylfurfural (HMF), acetate, or multiple different phenolic compounds in the acidic hydrolysis of polymeric carbohydrates [ 5 ]. FF stems from the dehydration of pentoses [ 6 ], while HMF originates from hexoses [ 7 ], resulting in varying furan ratios depending on the lignocellulosic biomass hydrolyzed. Furanic compounds are known to damage or alter DNA structures [ 1 , 8 ], damage cell walls and membranes [ 6 ], and inhibit growth and enzymatic activities [ 9 ] in multiple different microorganisms.…”

Section: Introductionmentioning

confidence: 99%

Bioconversion of Furanic Compounds by Chlorella vulgaris—Unveiling Biotechnological Potentials

Kriechbaum,

Spadiut,

Kopp

2024

Microorganisms

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Lignocellulosic biomass is abundant on Earth, and there are multiple acidic pretreatment options to separate the cellulose, hemicellulose, and lignin fraction. By doing so, the fermentation inhibitors 5-Hydroxymethylfurfural (HMF) and furfural (FF) are produced in varying concentrations depending on the hydrolyzed substrate. In this study, the impact of these furanic compounds on Chlorella vulgaris growth and photosynthetic activity was analyzed. Both compounds led to a prolonged lag phase in Chlorella vulgaris growth. While the photosynthetic yield Y(II) was not significantly influenced in cultivations containing HMF, FF significantly reduced Y(II). The conversion of 5-Hydroxymethylfurfural and furfural to 5-Hydroxymethyl-2-Furoic Acid and 2-Furoic Acid was observed. In total, 100% of HMF and FF was converted in photoautotrophic and mixotrophic Chlorella vulgaris cultivations. The results demonstrate that Chlorella vulgaris is, as of now, the first known microalgal species converting furanic compounds.

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“…In some organisms (6. ), conversion to furoic acid is the first step in a degradation pathway that allows the utilisation of furfural as a carbon source [ 61 ].…”

Section: Introductionmentioning

confidence: 99%

Improved furfural tolerance in Escherichia coli mediated by heterologous NADH-dependent benzyl alcohol dehydrogenases

Willson

Herman

Langer

et al. 2022

Biochemical Journal

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While lignocellulose is a promising source of renewable sugars for microbial fermentations, the presence of inhibitory compounds in typical lignocellulosic feedstocks, such as furfural, has hindered their utilisation. In Escherichia coli, a major route of furfural toxicity is the depletion of NADPH pools due to its use as a substrate by the YqhD enzyme that reduces furfural to its less toxic alcohol form. Here, we examine the potential of exploiting benzyl alcohol dehydrogenases as an alternative means to provide this same catalytic function but using the more abundant reductant NADH, as a strategy to increase the capacity for furfural removal. We determine the biochemical properties of three of these enzymes, from Pseudomonas putida, Acinetobacter calcoaceticus, and Burkholderia ambifaria, which all demonstrate furfural reductase activity. Furthermore, we show that the P. putida and B. ambifaria enzymes are able to provide substantial increases in furfural tolerance in vivo, by allowing more rapid conversion to furfuryl alcohol and resumption of growth. The study demonstrates that methods to seek alternative co-factor dependent enzymes can improve the intrinsic robustness of microbial chassis to feedstock inhibitors.

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Widespread distribution of hmf genes in Proteobacteria reveals key enzymes for 5-hydroxymethylfurfural conversion

Abstract: Graphical abstract

Cited by 11 publications

References 69 publications

Identification of a Phylogenetically Divergent Vanillate O-Demethylase from Rhodococcus ruber R1 Supporting Growth on Meta-Methoxylated Aromatic Acids

Identification of a Phylogenetically Divergent Vanillate O-Demethylase from Rhodococcus ruber R1 Supporting Growth on Meta-Methoxylated Aromatic Acids

Bioconversion of Furanic Compounds by Chlorella vulgaris—Unveiling Biotechnological Potentials

Improved furfural tolerance in Escherichia coli mediated by heterologous NADH-dependent benzyl alcohol dehydrogenases

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