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At least 19 recordsLinked to original sources

PubMed1978

Screening for lignin degrading bacteria by means of 14C-labelled lignins.

Several Nocardia and Pseudomonas spp., as well as some unidentified bacteria, isolated from lake water containing high loads of waste lignin, were tested for their capacity to release 14CO2 from specifically 14C-labelled dehydropolymer of coniferyl alcohol (DHP) or corn stalk lignins. The bacteria were selected according to their ability to degrade phenolic compounds. However, only some of them could release significant amounts of 14CO2 from the labelled lignin. The tested Nocardia spp. were more active than the Pseudomonas spp. and the unidentified bacteria. The most active strains belonged to N. autotrophica. These strains released CO2 significantly from the methoxyl group and transformed the other carbons from the phenylpropane skeleton of lignin also into CO2. Other less demethylating strains also released little CO2 from the other carbons of the lignin molecule. From corn stalk materials which were specifically labelled in the lignin part, only small amounts of labelled CO2 were released.

Biodegradation, Environmental↗

PubMed2025

The mhqPOD gene cluster in lignin-degrading Paenibacillus sp. B2 encodes a pathway for the degradation of lignin-derived 5,5'-di(dehydrovanillic acid) (DDVA).

Lignin-degrading bacteria Paenibacillus sp. B2, Agrobacterium sp. B1, and Ochrobactrum sp. each contain mhqO genes encoding ring cleavage dioxygenase enzymes whose biochemical function is unknown. Each of these strains was found to degrade the biphenyl-containing lignin fragment 5,5'-di(dehydrovanillic acid) (DDVA) on solid media. An operon of five mhq genes in Paenibacillus sp. B2 was analysed via gene expression using quantitative PCR, and all five genes were highly induced (400-1000-fold overexpression) by the presence of DDVA. Recombinant azoreductase MhqP was found to demethylate DDVA to its monodemethylated derivative. Hence, these genes are proposed to be responsible for DDVA degradation, via a pathway involving the same biochemical steps as that studied in Sphingobium lignivorans SYK-6, but using several unrelated genes. Decarboxylation of later pathway intermediate 5-carboxyvanillic acid in Paenibacillus sp. B2 is proposed to be catalysed by decarboxylase UbiD, whose gene is also upregulated in the presence of DDVA. Degradation of the other fragment 4-carboxy-2-hydroxypentadienoic acid is proposed to occur via hydratase UxuA, whose gene is also upregulated by DDVA, and 4-hydroxy-4-methyl-2-oxoglutarate aldolase.

Paenibacillus↗

PubMed1978

Bacterial decomposition of synthetic 14C-labeled lignin and lignin monomer derivatives.

Nocardia sp. which was isolated from soil is capable of degrading synthetic lignin and utilizing its monomer derivatives. Decomposition was monitored by measuring the 14CO2 evolved and O2 consumed, when the bacterium was grown on a medium containing specifically 14C-labeled ligning or monomer phenolic compounds as major carbon source. The time course of the 14CO2 release and O2 uptake indicates a significant depolymerization and utilization of lignin by the Nocardia sp.

Anisoles↗

PubMed1977

Degradation of natural and Kraft lignins by the microflora of soil and water.

The comparative rates of microbial degradation of 14C-lignin-labeled lignocelluloses and 14C-Kraft lignins were investigated using selected soil and water samples as sources of microorganisms. Natural lignocelluloses containing 14C primarily in their lignin components were prepared by feeding plants uniformly labeled L-[14C]phenylalanine through their cut stems. 14C-Kraft lignins were prepared by pulping lignin-labeled lignocelluloses. Rates of lignin biodegradation were determined by monitoring 14CO2 evolution from incubation mixtures over incubation periods of up to 1000 h. Observed rates of lignin degradation were slow in all cases. Kraft lignins appeared more resistant to microbial attack than natural lignins, even though they were decomposed more rapidly during the first 100-200 h of incubation. Similar degradation patterns were observed in both soil and water. Individual samples, however, varied greatly in their overall rates of degradation of either lignin type. A Kraft-lignin preparation was separated into a variety of molecular weight fractions by column chromatography on LH-20 Sephadex and the biodegradability of the different molecular weight fractions determined. The lower molecular weight fractions of the Kraft lignin were decomposed at a significantly faster rate by the microflora of soil than were the fractions of higher molecular weight.

Bacteria↗

PubMed2026

Addressing lignin composition and content via Arabidopsis arogenate dehydratase knockout and over-expression genotypes.

Following the down-selection of 14 Arabidopsis thaliana arogenate dehydratase (ADT) knockout and over-expression (OE) genotypes, the most highly contrasting quadruple knockout adt3/4/5/6 and ADT OE genotypes were subjected to proteomics, metabolomics, and scanning electron microscopy (SEM) analyses as needed, with results compared to Columbia wild-type (WT). The basal adt3/4/5/6 stem cross-sections, ∼70% lignin content reduced, exhibited buckled vessel cell walls and partially detached xylary fibers, in contrast to WT and ADT4m/5 m OE genotypes that did not. Anatomical defects primarily resulted from guaiacyl lignin level reductions in vessels with concomitant increased stem syringyl:guaiacyl (S/G) ratios. Phenylpropanoid and various upstream shikimate-chorismate pathway enzyme abundances, as well as specific monolignol oxidases (laccases/peroxidases), generally increased in adt3/4/5/6 at different stem and rosette leaf growth/development stages, relative to WT. Opposite effects were largely observed with the ADT5m OE genotype. By contrast, flavonoid and glucosinolate pathway enzyme amounts varied. Such enzyme abundance increases were overall unproductive as adt3/4/5/6 was unable to restore WT, ADT4 OE, ADT5 OE, ADT5m OE, and ADT4m/5 m OE secondary metabolite (lignin, phenylpropanoid, lignan, flavonoid, phenolic acid, and glucosinolate) levels. Conversely, ADT OE genotypes did not significantly increase programmed lignin levels or alter S/G compositions. In sum, proteomics analyses of adt3/4/5/6 and adt5 'perceived' that lignin and low molecular weight secondary metabolite amounts were not at 'programmed' levels as for WT and ADT OE genotypes but observed increases in relevant pathway protein abundances were futile. Notably though, proteomics analyses did not lead to predicting that lignin and associated biochemical pathways would have reduced metabolite levels, relative to WT and ADT OE genotypes. Genotype adt3/4/5/6, possibly the highest lignin level reduced genotype reported, did not utilize other phenolics to compensate. By contrast, the differential temporal and spatial deposition of cell wall oxidases again indicate the exquisite control over lignin deposition, and our lack of knowledge of precise lignin structure and assembly in subcellular regions of the lignified cell walls.

Lignin↗

PubMed1992

Reversible binding of the cooked food mutagen MeIQx to lignin-enriched preparations from wheat bran.

The binding of the mutagen 3,8-dimethyl-3H-imidazo[4,5-f]quinoxaline-2-amine (MeIQx) to various fibre preparations from wheat bran was studied. The physical structures of wheat bran and lignin-enriched preparations were determined by scanning electron microscopy. With increasing mutagen concentration from 0.5-16 micrograms/ml, the fraction of MeIQx bound to cellulase-treated lignin was nearly constant, for a certain lignin density. The binding between cellulase-treated lignin and MeIQx was reversible. Incubation temperature influenced the rate at which the equilibrium between lignin and MeIQx was established, but had less effect on the equilibrium itself. With increasing fibre densities and a constant mutagen concentration, complete binding was apparently reached at a high fibre density. This was illustrated by plotting the data according to Scatchard. Increased binding of the MeIQx was obtained with increased enrichment of lignin in different fibre preparations.

Dietary Fiber↗

PubMed2026

GA4+7 alleviates pear fruit semi-russeting partly by suppressing PRX-mediated lignin deposition.

Pear fruit semi-russeting is a surface disorder that frequently occurs during fruit development and significantly diminishes fruit appearance quality and commercial value. Although Gibberellin 4 + 7 (GA4+7) has been used to reduce fruit surface defects in horticultural crops, the physiological and molecular mechanisms underlying its inhibitory effect on pear fruit semi-russeting remain poorly understood. In this study, preharvest GA4+7 treatment of 'Cuiguan' pear significantly reduced russet coverage and lignin accumulation in mature fruit skin without adversely affecting fruit size, fruit shape index, or total soluble solids content. Integrated metabolomic and transcriptomic analyses revealed that GA4+7 treatment was associated with the repression of phenylpropanoid and lignin biosynthesis at both metabolic and transcriptional levels. Among the lignin-related differentially expressed genes, two class III peroxidase genes, PpyPRX22 and PpyPRX65, were strongly downregulated by both GA4+7 and bagging treatments. Both proteins localized to the cell wall, and transient expression assays in pear fruit skin supported positive roles for PpyPRX22 and PpyPRX65 in lignin deposition. Furthermore, dual-luciferase reporter assays combined with transient overexpression experiments suggested that several PpyMYB transcription factors may regulate PpyPRX expression and lignin accumulation, with PpyMYB138 and PpyMYB139 significantly activating PpyPRX22 and/or PpyPRX65 promoter activity. Taken together, these results suggest that GA4+7 alleviates pear fruit semi-russeting at least partly by reducing lignin deposition in the fruit skin, with PpyPRX22 and PpyPRX65 potentially contributing to this process.

Class III peroxidase↗

PubMed1975

Presence of soluble lignin-carbohydrate complexes in the bovine rumen.

The cell-free rumen liquor of a steer on a diet of spear grass has been shown to contain macromolecular substances in which carbohydrates and lignin-derived compounds are covalently bound to each other. The lignin-carbohydrate complexes are soluble at pH 7 or higher, but precipitate at pH 3. At the latter pH, small amounts of a polymer, assumed to be glycoprotein, remain in solution. Some of the lignin-carbohydrate linkages are broken by treatment with alkali. Treatment with 50mM sulphuric acid for a few minutes at room temperature converts part of the complex into an acetone-soluble product, which still contains both carbohydrate and lignin-derived compounds. The formation of soluble lignin-carbohydrate complexes by the action of rumen micro-organisms on the grass may account for the dissolution (and hence the apparent digestion) of about half of the total lignin-intake.

Acetone↗

PubMed1992

Catalytic mechanisms and regulation of lignin peroxidase.

Lignin peroxidase (LiP) is a fungal haemoprotein similar to the lignin-synthesizing plant peroxidases, but it has a higher oxidation potential and oxidizes dimethoxylated aromatic compounds to radical cations. It catalyses the degradation of lignin models but in vitro the outcome is net lignin polymerization. LiP oxidizes veratryl alcohol to radical cations which are proposed to act by charge transfer to mediate in the oxidation of lignin. Phenolic compounds are, however, preferentially oxidized, but transiently inactivate the enzyme. Analysis of the catalytic cycle of LiP shows that in the presence of veratryl alcohol the steady-state turnover intermediate is Compound II. We propose that veratryl alcohol is oxidized by the enzyme intermediate Compound I to a radical cation which now participates in charge-transfer reactions with either veratryl alcohol or another reductant, when present. Reduction of Compound II to native state may involve a radical product of veratryl alcohol or radical product of charge transfer. Phenoxy radicals, by contrast, cannot engage in charge-transfer reactions and reaction of Compound II with H2O2 ensues to form the peroxidatically inactive intermediate, Compound III. Regulation of LiP activity by phenolic compounds suggests feedback control, since many of the products of lignin degradation are phenolic. Such control would lower the concentration of phenolics relative to oxygen and favour degradative ring-opening reactions.

Benzyl Alcohols↗

PubMed1990

Cloning and expression of a lignin peroxidase gene from Streptomyces viridosporus in Streptomyces lividans.

A lignin peroxidase gene was cloned from Streptomyces viridosporus T7A into Streptomyces lividans TK64 in plasmid pIJ702. BglII-digested genomic DNA (4-10 kb) of S. viridosporus was shotgun-cloned into S. lividans after insertion into the melanin (mel+) gene of pIJ702. Transformants expressing pIJ702 with insert DNA were selected based upon the appearance of thiostrepton resistant (tsrr)/mel-colonies on regeneration medium. Lignin peroxidase-expressing clones were isolated from this population by screening of transformants on a tsr-poly B-411 dye agar medium. In the presence of H2O2 excreted by S. lividans, colonies of lignin peroxidase-expressing clones decolorized the dye. Among 1000 transformants screened, 2 dye-decolorizing clones were found. One, pIJ702/TK64.1 (TK64.1), was further characterized. TK64.1 expressed significant extracellular 2,4-dichlorophenol (2.4-DCP) peroxidase activity (= assay for S. viridosporus lignin peroxidase). Under the cultural conditions employed, plasmidless S. lividans TK64 had a low background level of 2.4-DCP oxidizing activity. TK64.1 excreted an extracellular peroxidase not observed in S. lividans TK64, but similar to S. viridosporus lignin peroxidase ALip-P3, as shown by activity stain assays on nondenaturing polyacrylamide gels. The gene was located on a 4 kb fragment of S. viridosporus genomic DNA. When peroxidase-encoding plasmid, pIJ702.LP, was purified and used to transform three different S. lividans strains (TK64, TK23, TK24), all transformants tested decolorized poly B-411. When grown on lignocellulose in solid state processes, genetically engineered S. lividans TK64.1 degraded the lignocellulose slightly better than did S. lividans TK64. This is the first report of the cloning of a bacterial gene coding for a lignin-degrading enzyme.

Cloning, Molecular↗

PubMed1992

Haloperoxidase activity of Phanerochaete chrysosporium lignin peroxidases H2 and H8.

Monochlorodimedone (MCD), commonly used as a halogen acceptor for haloperoxidase assays, was oxidized by hydrogen peroxide in the presence of lignin peroxidase isoenzymes H2 and H8. When oxidized, it produced a weak absorption band with an intensity that varied with pH. This absorbance was used as a simple method for the product analysis because it disappeared when MCD was brominated or chlorinated. We assessed the activity of the lignin peroxidases for oxidation of bromide by measuring the bromination of MCD, the formation of tribromide, the bromide-mediated oxidation of glutathione, and the bromide-mediated catalase-like activity. We analyzed the reaction products of MCD and the halide-mediated oxidation of glutathione when bromide was replaced by chloride. These enzymes demonstrated no significant activity for oxidation of chloride. Unlike other peroxidases, the lignin peroxidases exhibited similar pH-activity curves for the iodide and bromide oxidations. The optimum pH for activity was about 2.5. Surprisingly, this pH dependence of lignin peroxidase activity for the halides was nearly the same in the reactions with hydrogen donors, such as hydroquinone and guaiacol. The results suggested that protonation of the enzymes with pKa approximately 3.2 is necessary for the catalytic function of lignin peroxidases, irrespective of whether the substrates are electron or hydrogen donors. These unique reaction profiles of lignin peroxidases are compared to those of other peroxidases, such as lactoperoxidase, bromoperoxidase, chloroperoxidase, and horseradish peroxidase. Isozyme H2 was more active than isozyme H8, but isozyme H8 was more stable at very acidic pH.

Basidiomycota↗

PubMed2025

Factors underlying a latitudinal gradient in the S/G lignin monomer ratio in natural poplar variants.

The chemical composition of wood plays a pivotal role in the adaptability and structural integrity of trees. However, few studies have investigated the environmental factors that determine lignin composition and its biological significance in plants. Here, we examined the lignin syringyl-to-guaiacyl (S/G) ratio in members of a Populus trichocarpa population sourced from their native habitat and conducted a genome wide association study to identify genes linked to lignin formation. Our results revealed many significant associations, suggesting that lignin biosynthesis is a complex polygenic trait. Additionally, we found an increase in the S/G ratio from northern to southern geographic origin of the trees sampled, along with a corresponding metabolic and transcriptional reprogramming of xylem cell wall biosynthesis. Further molecular analysis identified a mutation in a cell wall laccase genetically associated with higher S/G ratios that predominate in trees from warmer lower latitudes. Collectively, our findings suggest that lignin heterogeneity arises from an evolutionary process enabling poplar adaptation to different climatic challenges.

Populus↗

PubMed1992

Comparison of bromine and permanganate as ultrastructural stains for lignin in plants infected by the fungus Colletotrichum lagenarium.

Transmission electron microscopy (TEM) and energy dispersive X-ray microanalysis (EDS) were used to localize manganese from KMnO4, and bromine, as ultrastructural stains for lignin in an herbaceous plant. The Spookie cultivar of pumpkin is susceptible to infection by the fungus Colletotrichum lagenarium and served as a model system to compare the Br and KMnO4 techniques. Bromine was used in a fixation/staining procedure, and in separate experiments, KMnO4 was used as either a fixative or as a postsection stain. The technique for using bromine was modified from the woody plant procedure by adding a paraformaldehyde prefixation step. With the bromine procedure, cell walls were well-preserved, but the cytoplasm was heavily extracted. The KMnO4 procedures produced well-fixed cytoplasm, but with some staining artifacts. With all procedures, EDS dot mapping demonstrated lignin deposition in the cell walls specifically associated with sites of fungal infection. Lignin was also localized in secondary walls of tracheary elements, sites known to be highly lignified. The bromine procedure provided the most specific localization of lignin with a minimum of artifact. The specific applications of these stains provided data on the ultrastructural localization of lignin which contributed to the elucidation of its role in the interactions between pathogenic fungi in both their resistant and susceptible plant hosts.

Bromine↗

PubMed1990

Multiple lignin peroxidases of Phanerochaete chrysosporium INA-12.

Nine proteins with lignin peroxidase activity were separated from cultures of Phanerochaete chrysosporium INA-12 in glycerol as carbon source and non-nitrogen limited. Four lignin peroxidase isozymes (4, 5, 8, 9) were purified and characterized. Although differences in kinetic parameters could be shown, antibody reaction showed homology between isozymes. However, thermal stability studied, peptide mapping results, and N-terminal sequence analyses established a higher degree of homology between isozymes 4/5 and 8/9 types. Protein characterization and kinetic data indicate that lignin peroxidase isozymes 4, 5, 8, and 9 differ from described isozymes in strain BKM. The higher specific activity of lignin peroxidase isozymes in cultures with glycerol than in nitrogen-starved cultures accounts for the higher lignin peroxidase activity obtained in these conditions.

Amino Acid Sequence↗

PubMed2024

Genetic modification of the shikimate pathway to reduce lignin content in switchgrass (Panicum virgatum L.) significantly impacts plant microbiomes.

UNLABELLED: Switchgrass (Panicum virgatum L.) is considered a sustainable biofuel feedstock, given its fast-impact growth, low input requirements, and high biomass yields. Improvements in bioenergy conversion efficiency of switchgrass could be made by reducing its lignin content. Engineered switchgrass that expresses a bacterial 3-dehydroshikimate dehydratase (QsuB) has reduced lignin content and improved biomass saccharification due to the rerouting of the shikimate pathway towards the simple aromatic protocatechuate at the expense of lignin biosynthesis. However, the impacts of this QsuB trait on switchgrass microbiome structure and function remain unclear. To address this, wild-type and QsuB-engineered switchgrass were grown in switchgrass field soils, and samples were collected from inflorescences, leaves, roots, rhizospheres, and bulk soils for microbiome analysis. We investigated how QsuB expression influenced switchgrass-associated fungal and bacterial communities using high-throughput Illumina MiSeq amplicon sequencing of ITS and 16S rDNA. Compared to wild-type, QsuB-engineered switchgrass hosted different microbial communities in roots, rhizosphere, and leaves. Specifically, QsuB-engineered plants had a lower relative abundance of arbuscular mycorrhizal fungi (AMF). Additionally, QsuB-engineered plants had fewer Actinobacteriota in root and rhizosphere samples. These findings may indicate that changes in the plant metabolism impact both AMF and Actinobacteriota similarly or potential interactions between AMF and the bacterial community. This study enhances understanding of plant-microbiome interactions by providing baseline microbial data for developing beneficial bioengineering strategies and by assessing nontarget impacts of engineered plant traits on the plant microbiome. IMPORTANCE: Bioenergy crops provide an important strategy for mitigating climate change. Reducing the lignin in bioenergy crops could improve fermentable sugar yields for more efficient conversion into bioenergy and bioproducts. In this study, we assessed how switchgrass engineered for low lignin impacted aboveground and belowground switchgrass microbiome. Our results show unexpected reductions in mycorrhizas and actinobacteria in belowground tissues, raising questions on the resilience and function of genetically engineered plants in agricultural systems.

Panicum↗

PubMed2026

DfCAD16 controls guaiacyl lignin biosynthesis during shoot development in Dendrocalamus farinosus.

Although bamboo can be an ideal raw material for pulp and paper industry, the depolymerization of its complex polymers needs to be facilitated. The deposition of lignin is influenced by cinnamyl alcohol dehydrogenase (CAD), an enzyme that catalyzes the formation of monolignol precursors. Here, we identified 18 DfCAD genes in Dendrocalamus farinosus and revealed using bioinformatics methods, DfCAD16 functions as the primary enzyme in the synthesis pathway of guaiacyl (G)-lignin. Phenotypic analysis of plants overexpression DfCAD16 exhibited remarkable increasing in G-lignin. Furthermore, we demonstrated that an R2R3-type MYB transcription factor DfMYB12 could directly bind to the promoter region of DfCAD16 and activate its expression both in vitro and in vivo. Our findings revealed that DfMYB12-DfCAD16 is a key regulatory factor governing G-lignin biosynthesis in D. farinosus. These insights can be used for improving bamboo varieties for pulp production.

Lignin↗

PubMed2026

Abscisic acid promotes RBOH-dependent reactive oxygen species production and lignin biosynthesis in pears via the PuABI5-PuMYB169 module.

Pear stone cell lignification, a critical determinant of fruit texture and quality, is regulated by developmental and environmental cues, with abscisic acid (ABA) playing a central role. However, the molecular mechanisms underlying its role in reactive oxygen species (ROS)-mediated lignification remain unclear. Here, we show that PuABI5, a key component in ABA signaling, directly combines with PuMYB169, the master regulator of stone cell lignification, to modulate ROS production and lignin biosynthesis in pear fruit. Exogenous application of ABA enhances H2O2 and lignin accumulation in both pear fruits and calli, and ABA-activated PuABI5 positively regulates stone cell lignification. We demonstrate that ABA-induced PuABI5 binds directly to the PuMYB169 promoter and activates its expression to promote the transcription of PuRBOHF and lignin-related genes, thereby enhancing ROS production and lignin accumulation. Notably, PuABI5 interacted with PuMYB169 to enhance the induction of PuRBOHF expression, leading to elevated levels of H2O2, which feedback to strengthen the interaction between PuABI5 and PuMYB169. Collectively, our findings elucidate that ABA induces ROS-mediated lignification of stone cells in pears by activating the PuABI5-PuMYB169 transcriptional module.

Lignin↗

PubMed1978

The lignin fraction of plant cell walls.

Methods are discussed for determining lignin in plant cell walls. The increase in apparent lignin content that may occur as a result of artifacts produced during food preparation is also discussed. The phenolic components, including lignin, of cell walls separated from 12 vegetable, fruit, and cereal foods are determined. Wheat bran, on a fresh weight basis, had a high cell wall content (48.6%) compared with the vegetables and fruit whose contents ranged from 1.0 to 6.0%. Wheat bran and spinach cell walls had the highest lignin contents (11.4 and 4.4%, respectively) and the lowest degradabilities (35.8 and 39.6%, respectively) as determined by a cellulase technique. Cell walls of spinach, beetroot, sweet corn, pineapple, and wheat bran contained the phenolic acids (ferulic, p-coumaric, and diferulic) bound to polysaccharide components. Cell walls of cabbage, Brussels sprout, celery, cauliflower, green bean, carrot, and pea contained only traces of these acids.

Cell Wall↗