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PubMed1993

Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. II. Partial sequences, peptide maps, and amino acid and carbohydrate compositions.

The basidiomycete Trametes versicolor, a white-rot fungus and potent degrader of lignin, produces multiple forms of extracellular peroxidases. Nine of these forms, six lignin peroxidases and three manganese(II) peroxidases, purified as described in the preceding paper, were characterized by amino-terminal sequencing, amino acid analyses, carbohydrate analyses, or peptide mapping. For two of the lignin peroxidase forms, tryptic peptides were isolated and sequenced to an extent corresponding to about 40 and 30%, respectively, of the primary structure. Eight of the nine peroxidases investigated were found to possess unique amino-terminal regions. A comparison of the sequences shows 57% of the residues to be identical, indicating a common ancestry for the lignin peroxidase and the manganese(II) peroxidase. The degree of identity among the five lignin peroxidases is about 80% and among the three manganese(II) peroxidases about 70%. Pairwise comparisons of the sequences disclosed that some of the lignin peroxidases are very closely related, either identical or differing only in a single amino acid residue of the thirty-five investigated. These close relationships are also supported by peptide mapping and by similarities in amino acid compositions. Tyr is absent in all isozymes. Lignin and manganese(II) peroxidases showed the presence of glucosamine and mannose in an amount corresponding to 3 to 6% of the molecular mass of the proteins. The carbohydrate compositions are compatible with the presence of 1, 2, and 3 sites of N-glycosylation. The results obtained strongly suggest that the complexity in the peroxidase pattern displayed by the fungus (T. Johansson and P.O. Nyman, Arch. Biochem. Biophys. 300, 49-56, 1993) can largely be accounted for by a heterogeneity at the gene level, probably in the form of multiple structural genes. Two recently published genes from genomic clones of T. versicolor are identical in sequence to two of the lignin peroxidases characterized here.

Amino Acid Sequence↗
PubMed1984

Production of useful modified lignin polymers by bioconversion of lignocellulose with Streptomyces.

Lignin degrading strains of Streptomyces were grown on lignocelluloses from a variety of plant sources. These actinomycetes readily degraded the lignin present in the residues and released a major portion of the lignin into the growth medium as a water soluble, modified polymer. The polymer, an acid precipitable polyphenolic lignin (APPL), was recovered from spent culture media by acid precipitation or dialysis/lyophilization. APPL's were shown to be mostly free of nonlignin components. As compared to native lignin they were more oxidized, were especially enriched in phenolic hydroxyl groups, and were significantly reduced in methoxyl groups. The yield of APPL from different lignocelluloses correlated with their biodegradability. Grasses such as corn stover were the optimal lignocellulose type for APPL production by Streptomyces. In contrast white-rot fungi produced only small amounts of APPL as they decomposed lignin. A solid state bioconversion process was developed using Streptomyces viridosporus T7A to produce APPL from corn stover lignocellulose in yields >or= 30% of the initial lignin present in the substrate. APPL produced by S. viridosporus was examined for its properties and possible use as an antioxidant. The APPL was shown to have good antioxidant properties after mild chemical treatment to reduce the alpha-carbonyl groups present in the APPL. Oxidation of the APPL with hydroxyl radical (OH(*)) further improved its antioxidant properties probably as the result of aromatic ring hydroxylation reactions. As compared with currently used commercial antioxidants, the modified APPL was thought to be competitive when economics of production was considered. Native lignin on the other hand was shown to exhibit no antioxidant properties, even after reduction and/or oxidation.

Journal Article↗
PubMed2001

Comparison of two assay procedures for lignin peroxidase.

The most widely accepted assay for detecting lignin peroxidase, based on the oxidation of veratryl alcohol to veratraldehyde, suffers from some drawbacks. At 310 nm, the wavelength at which the assay is performed, some other materials like lignins, quinonic compounds and aromatics also exhibit strong absorbance thus interfering with the estimation when present in the media. The present study reports the lignin peroxidase production by some white rot fungi under different nutritional conditions. The veratryl alcohol oxidation assay procedure for lignin peroxidase has been compared with another method based on the oxidation of the dye azure B involving absorbance measurements in the visible range. The latter method proved to be much more advantageous over the veratryl alcohol oxidation method, in media supplemented with malt extract, lignin preparations and agricultural residues. The enzyme production by veratryl alcohol assay could be detected only in mineral salts broth. By the azure B assay the enzyme activity was detected in all the media tested. The supplements gave varied response in different media. Veratryl alcohol enhanced the enzyme production in malt extract broth and mineral salts malt extract broth. Among the lignin preparations Indulin AT increased the lignin peroxidase titres from 2 to 20 fold in different fungi. Similarly, wheat straw supplemented in mineral salts broth and malt extract broth, separately, strongly stimulated the lignin peroxidase production. The above studies revealed that azure B assay may act as a substitute or equivalent method.

Journal Article↗
PubMed1999

Structural alterations of lignins in transgenic poplars with depressed cinnamyl alcohol dehydrogenase or caffeic acid O-methyltransferase activity have an opposite impact on the efficiency of industrial kraft pulping

We evaluated lignin profiles and pulping performances of 2-year-old transgenic poplar (Populus tremula x Populus alba) lines severely altered in the expression of caffeic acid/5-hydroxyferulic acid O-methyltransferase (COMT) or cinnamyl alcohol dehydrogenase (CAD). Transgenic poplars with CAD or COMT antisense constructs showed growth similar to control trees. CAD down-regulated poplars displayed a red coloration mainly in the outer xylem. A 90% lower COMT activity did not change lignin content but dramatically increased the frequency of guaiacyl units and resistant biphenyl linkages in lignin. This alteration severely lowered the efficiency of kraft pulping. The Klason lignin level of CAD-transformed poplars was slightly lower than that of the control. Whereas CAD down-regulation did not change the frequency of labile ether bonds or guaiacyl units in lignin, it increased the proportion of syringaldehyde and diarylpropane structures and, more importantly with regard to kraft pulping, of free phenolic groups in lignin. In the most depressed line, ASCAD21, a substantially higher content in free phenolic units facilitated lignin solubilization and fragmentation during kraft pulping. These results point the way to genetic modification of lignin structure to improve wood quality for the pulp industry.

Journal Article↗
PubMed1989

Modification of Lignins by Growing Cells of the Sulfate-Reducing Anaerobe Desulfovibrio desulfuricans.

The anaerobic sulfate-reducing bacterium Desulfovibrio desulfuricans was grown on medium supplemented with either Kraft lignin or lignosulfonate. Only lignosulfonate contributed to the growth of D. desulfuricans cells, by replacing sulfate, a natural electron acceptor for this microorganism. Kraft lignin added to the culture medium could not substitute for lactate or sulfate, both necessary culture medium components. However, it was found to enhance the viability of D. desulfuricans cells. When changes occurring in lignin during growth of Desulfovibrio cultures were monitored, it was found that both lignin preparations could be partially depolymerized. Spectrophotometric and elemental analysis of biologically treated lignins suggested that both the polyphenolic backbone and lignin functional groups were affected by D. desulfuricans. After treatment, a twofold increase in the sulfur content of Kraft lignin and a minor decrease (14%) in the sulfur content of lignosulfonate were observed. After biological treatment, Kraft lignin and lignosulfonate both bound larger quantities of heavy metals.

Journal Article↗
PubMed1992

Lignin Peroxidase Activity Is Not Important in Biological Bleaching and Delignification of Unbleached Kraft Pulp by Trametes versicolor.

The discovery in 1983 of fungal lignin peroxidases able to catalyze the oxidation of nonphenolic aromatic lignin model compounds and release some CO(2) from lignin has been seen as a major advance in understanding how fungi degrade lignin. Recently, the fungus Trametes versicolor was shown to be capable of substantial decolorization and delignification of unbleached industrial kraft pulps over 2 to 5 days. The role, if any, of lignin peroxidase in this biobleaching was therefore examined. Several different assays indicated that T. versicolor can produce and secrete peroxidase proteins, but only under certain culture conditions. However, work employing a new lignin peroxidase inhibitor (metavanadate ions) and a new lignin peroxidase assay using the dye azure B indicated that secreted lignin peroxidases do not play a role in the T. versicolor pulp-bleaching system. Oxidative activity capable of degrading 2-keto-4-methiolbutyric acid (KMB) appeared unique to ligninolytic fungi and always accompanied pulp biobleaching.

Journal Article↗
PubMed1994

Effect of Penicillium chrysogenum on Lignin Transformation.

A strain of Penicillium chrysogenum has been isolated from pine forest soils in Tenerife (Canary Islands). This strain was capable of utilizing hydroxylated and nonhydroxylated aromatic compounds, in particular cinnamic acid, as its sole carbon source. In an optimum medium with high levels of nitrogen (25.6 mM) and low levels of glucose (5.5 mM), it was able to decolorize Poly B-411 and to transform kraft, organosolv, and synthetic dehydrogenative polymerisate lignins. After 30 days of incubation, the amount of recovered kraft lignin was reduced to 83.5 and 91.3% of that estimated for uninoculated controls by spectrophotometry and klason lignin, respectively. At the same time, the pattern of molecular mass distribution of the lignin remaining in cultures was changed. The amount of organosolv lignin recovered from cultures was reduced to 90.1 and 94.6% of the initial amount as evaluated by spectrophotometry and klason lignin, respectively. About 6% of total applied radioactivity of OCH(3)-organosolv lignin was recovered as CO(2) after 30 days of incubation, and 18.5% of radioactivity from insoluble OCH(3)-organosolv lignin was solubilized. After 26 days of incubation, 2.9% of C-beta-dehydrogenative polymerisate and 4.1% of C-ring-dehydrogenative polymerisate evolved as CO(2).

Journal Article↗
PubMed1990

Nitrogen-deregulated mutants of Phanerochaete chrysosporium--a lignin-degrading basidiomycete.

Two nitrogen-deregulated mutants of Phanerochaete chrysosporium, der8-2 and der8-5, were isolated by subjecting wild type conidia to gamma irradiation, plating on Poly-R medium containing high levels of nitrogen, and identifying colonies that are able to decolorize Poly-R. The mutants showed high levels of ligninolytic activity (14C-synthetic lignin----14CO2), and lignin peroxidase, manganese peroxidase and glucose oxidase activities in both low nitrogen (2.4 mM) and high nitrogen (24 mM) media. The wild type on the other hand displayed these activities in low nitrogen medium but showed little or no activities in high nitrogen medium. Fast protein liquid chromatographic analyses showed that the wild type as well as the der mutants produce three major lignin peroxidase peaks (designated L1, L2 and L3) with lignin peroxidase activity in low nitrogen medium. Furthermore, in low nitrogen medium, mutant der8-5 produced up to fourfold greater lignin peroxidase activity than that produced by the wild type. In high nitrogen medium, the wild type produced no detectable lignin peroxidase peaks whereas the mutants produced peaks L1 and L2, but not L3, and a new lignin peroxidase protein peak designated LN. Mutants der8-2 and der8-5 also produced high levels of glucose oxidase, an enzyme known to be associated with secondary metabolism and an important source of H2O2 in ligninolytic cultures, both in low and high nitrogen media. In contrast, the wild type produced high levels of glucose oxidase in low nitrogen medium and only trace amounts of this enzyme in high nitrogen medium.(ABSTRACT TRUNCATED AT 250 WORDS)

Basidiomycota↗
PubMedDate not supplied

Lignin biodegradation by the ascomycete Chrysonilia sitophila.

The lignin biodegradation process has an important role in the carbon cycle of the biosphere. The study of this natural process has developed mainly with the use of basidiomycetes in laboratory investigations. This has been a logical approach since most of the microorganisms involved in lignocellulosic degradation belong to this class of fungi. However, other microorganisms such as ascomycetes and also some bacteria, are involved in the lignin decaying process. This work focuses on lignin biodegradation by a microorganism belonging to the ascomycete class, Chrysonilia sitophila. Lignin peroxidase production and characterization, mechanisms of lignin degradation (lignin model compounds and lignin in wood matrix) and biosynthesis of veratryl alcohol are outstanding. Applications of C. sitophila for effluent treatment, wood biodegradation and single-cell protein production are also discussed.

Ascomycota↗
PubMed1989

Biomimetic oxidation of nonphenolic lignin models by Mn(III): new observations on the oxidizability of guaiacyl and syringyl substructures.

Mn(III) is a one-electron oxidant, produced in vivo by the Mn peroxidases of white-rot fungi, and thought to be involved in lignin degradation by these organisms. However, Mn(III) has not been shown to oxidize the major nonphenolic substructures of lignin under mild conditions. We have used Mn(III) acetate as a biomimetic model for enzymatically generated Mn(III), and report that low concentrations of this oxidant suffice to oxidize nonphenolic lignin models at physiological temperatures and pH values. Under these conditions, the monomeric lignin model veratryl alcohol was oxidized to veratraldehyde, and the diarylpropane model 1-(3,4-dimethoxyphenyl)-2-phenylpropanol was oxidatively cleaved to veratraldehyde, 1-phenylethanol, and acetophenone. In an attempt to identify other lignin models that might be oxidized by Mn(III) more rapidly, we compared the rates at which Mn(III) was reduced by two guaiacyl models, veratryl alcohol and 1-(3-methoxy-4-isopropoxyphenyl)ethanol, vs two syringyl models, 3,4,5-trimethoxybenzyl alcohol and 1-(3,5-dimethoxy-4-isopropoxyphenyl)ethanol. The results were the opposite of those predicted: the syringyl models were oxidized slower than the guaiacyl models by Mn(III). To investigate the basis for this unexpected result, we recorded the visible absorption spectra of charge-transfer complexes prepared between each of the lignin models and an electron acceptor, tetracyanoethylene or p-chloranil. The results, in general agreement with the kinetic findings, showed that the nonphenolic syringyl lignin models had higher ionization potentials than the guaiacyl models.

Biodegradation, Environmental↗
PubMed1991

In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium.

Homogeneous manganese peroxidase catalyzed the in vitro partial depolymerization of four different 14C-labeled synthetic lignin preparations. Gel permeation profiles demonstrated significant depolymerization of 14C-sidechain-labeled syringyl lignin, a 14C-sidechain-labeled syringyl-guaiacyl copolymer (angiosperm lignin), and depolymerization of 14C-sidechain- and 14C-ring-labeled guaiacyl lignins (gymnosperm lignin). 3,5-Dimethoxy-1,4-benzo-quinone, 3,5-dimethoxy-1,4-hydroquinone, and syringylaldehyde were identified as degradation products of the syringyl and syringyl-guaiacyl lignins. These results suggest that manganese peroxidase plays a significant role in the depolymerization of lignin by Phanerochaete chrysosporium.

Basidiomycota↗
PubMed2004

Characterization of the radical scavenging activity of lignins--natural antioxidants.

The present work is devoted to studies of the radical scavenging properties of lignins, which are recognized as efficient antioxidants of natural origin. Radical scavenging efficiency of a series of lignins isolated from deciduous and coniferous wood species and 10 lignin related monomeric compounds were examined against 1,1-diphenyl-2-picrylhydrazyl (DPPH*) radical in homogeneous conditions using ESR and spectrophotometry methods. Some structure-activity relationships are proposed, pointing out the importance of the non-etherified OH phenolic groups, ortho-methoxy groups, hydroxyl groups and the double bond between the outermost carbon atoms in the side chain for increasing scavenger activity. Analysis of rate constants for the lignins-DPPH* interaction revealed the contribution of polymer molecular weight and pi-polyconjugation systems. The pi-conjugation systems of lignins operate as catalysts/activators of the interaction with DPPH*. Heterogeneity in terms of component composition (carbohydrate admixtures) and polydispersity is the factor which can decrease drastically the antioxidant efficiency of isolated lignins. The connection of the antibacterial effect of kraft lignin with radical scavenging activity of its soluble fraction was assumed.

Antioxidants↗
PubMed2006

Physico-chemical characterization of lignins from different sources for use in phenol-formaldehyde resin synthesis.

During the last decades lignin has been investigated as a promising natural alternative to petrochemicals in phenol-formaldehyde (PF) resin production, due to their structural similarity. Physico-chemical characterization of three types of lignin, namely kraft pine lignin (L1), soda-anthraquinone flax lignin (L2), and ethanol-water wild tamarind lignin (L3) has been evaluated to determine which one is the most suitable chemical structure for above purpose. Characterization has been performed using Fourier transform infrared spectroscopy (FT-IR) and proton nuclear magnetic resonance spectrometry ((1)H NMR) to analyse the chemical structure, gel permeation chromatography (GPC) for determining molecular weight (MW) and molecular weight distribution (MWD), differential scanning calorimetry (DSC) to measure the glass transition temperature and thermogravimetric analysis (TGA) to follow the thermal degradation. Both structural and thermal characteristics suggest that kraft pine lignin (L1) would be a better phenol (P) substitute in the synthesis of lignin-phenol-formaldehyde (LPF) resins, as it presents higher amounts of activated free ring positions, higher MW and higher thermal decomposition temperature.

Calorimetry, Differential Scanning↗
PubMed2004

Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin.

The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG II or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG II also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T. reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin.

Adsorption↗
PubMed2006

Inhibition of cellulase, xylanase and beta-glucosidase activities by softwood lignin preparations.

The conversion of lignocellulosic biomass to fuel ethanol typically involves a disruptive pretreatment process followed by enzyme-catalyzed hydrolysis of the cellulose and hemicellulose components to fermentable sugars. Attempts to improve process economics include protein engineering of cellulases, xylanases and related hydrolases to improve their specific activity or stability. However, it is recognized that enzyme performance is reduced during lignocellulose hydrolysis by interaction with lignin or lignin-carbohydrate complex (LCC), so the selection or engineering of enzymes with reduced lignin interaction offers an alternative means of enzyme improvement. This study examines the inhibition of seven cellulase preparations, three xylanase preparations and a beta-glucosidase preparation by two purified, particulate lignin preparations derived from softwood using an organosolv pretreatment process followed by enzymatic hydrolysis. The two lignin preparations had similar particle sizes and surface areas but differed significantly in other physical properties and in their chemical compositions determined by a 2D correlation HSQC NMR technique and quantitative 13C NMR spectroscopy. The various cellulases differed by up to 3.5-fold in their inhibition by lignin, while the xylanases showed less variability (< or = 1.7-fold). Of all the enzymes tested, beta-glucosidase was least affected by lignin.

Cellulases↗
PubMed2001

Elucidation of new structures in lignins of CAD- and COMT-deficient plants by NMR.

Studying lignin-biosynthetic-pathway mutants and transgenics provides insights into plant responses to perturbations of the lignification system, and enhances our understanding of normal lignification. When enzymes late in the pathway are downregulated, significant changes in the composition and structure of lignin may result. NMR spectroscopy provides powerful diagnostic tools for elucidating structures in the difficult lignin polymer, hinting at the chemical and biochemical changes that have occurred. COMT (caffeic acid O-methyl transferase) downregulation in poplar results in the incorporation of 5-hydroxyconiferyl alcohol into lignins via typical radical coupling reactions, but post-coupling quinone methide internal trapping reactions produce novel benzodioxane units in the lignin. CAD (cinnamyl alcohol dehydrogenase) downregulation results in the incorporation of the hydroxycinnamyl aldehyde monolignol precursors intimately into the polymer. Sinapyl aldehyde cross-couples 8-O-4 with both guaiacyl and syringyl units in the growing polymer, whereas coniferyl aldehyde cross-couples 8-O-4 only with syringyl units, reflecting simple chemical cross-coupling propensities. The incorporation of hydroxycinnamyl aldehyde and 5-hydroxyconiferyl alcohol monomers indicates that these monolignol intermediates are secreted to the cell wall for lignification. The recognition that novel units can incorporate into lignins portends significantly expanded opportunities for engineering the composition and consequent properties of lignin for improved utilization of valuable plant resources.

Alcohol Oxidoreductases↗
PubMed1999

Solid-state spectroscopic analysis of lignins from several Austral hardwoods.

In order to gain information about lignin molecular characteristics with a direct bearing on the remarkable susceptibility of some Austral hardwoods to biological delignification, milled-wood lignins were isolated and analyzed by spectroscopic techniques in the solid state. Cross polarization and magic-angle spinning 13C nuclear magnetic resonance (13C CPMAS NMR) and Fourier-transform infrared (FTIR) spectra of the lignin preparations were obtained. The most diagnostic peaks were assigned and quantified as percentages of the total spectral area, and the differences observed discussed in terms of lignin composition. The spectral patterns obtained revealed that the woods from Gevuina avellana, Eucryphia cordifolia and Nothofagus dombeyii have lignin with high syringyl/guaiacyl ratio, as evidenced by relative areas of 13C NMR signals at 153 and 148 ppm, and FTIR bands at 1,335 and 1,275 cm-1. The presence of syringyl-rich lignins, characterized by lower redox potential and condensation degree than guaiacyl-rich lignins, could be a structural factor contributing to the ease of extensive delignification of these woods by white-rot fungi.

Chile↗
PubMed2003

Lignin distribution in wood cell walls determined by TEM and backscattered SEM techniques.

The lignin distribution in cell walls of spruce and beech wood was determined by high-voltage transmission-electron-microscopy (TEM) in sections stained with potassium permanganate as well as by field-emission-scanning-electron-microscopy (FE-SEM) combined with a back-scattered electron detector on mercurized specimens. The latter is a new technique based on the mercurization of lignin and the concomitant visualization of mercury by back-scattered electron microscopy (BSE). Due to this combination it was possible to obtain a visualized overview of the lignin distribution across the different layers of the cell wall. To our knowledge, this combined method was used the first time to analyse the lignin distribution in cell walls. In agreement with previous work the highest lignin levels were found in the compound middle lamella and the cell corners. Back-scattered FE-SEM allows the lignin distribution in the pit membrane of bordered pits as well as in the various cell wall layers to be shown. In addition, by using TEM as well as SEM we observed that lignin closely follows the cellulose microfibril orientation in the secondary cell wall. From these observations, we conclude that the polymerisation of monolignols is affected by the arrangement of the polysaccharides which constitute the cell wall.

Cell Wall↗