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At least 199 records · Page 11Linked to original sources
PubMed2000

An alpha-glucuronidase of Schizophyllum commune acting on polymeric xylan.

The main alpha-glucuronidase (EC 3.2.1.131) of the fungus Schizophyllum commune was purified to homogeneity using standard chromatographic methods; anion exchange, hydrophobic interaction chromatography and gel filtration. The enzyme had a molecular mass of 125 kDa as determined by SDS-polyacrylamide gel electrophoresis and a pI value of 3.6 according to isoelectric focusing. The N-terminal amino acid sequence of the S. commune alpha-glucuronidase did not show any homology with other alpha-glucuronidases. It exhibited maximal activity at pH values from 4.5 to 5.5 and was stable for 24 h between pH 6 and 8 at 40 degrees C. The highest temperature at which the enzyme retained its full activity for 24 h at pH 5.8 was 40 degrees C. The alpha-glucuronidase of S. commune was able to remove almost all 4-O-methylglucuronic acid groups from water-soluble polymeric softwood arabinoglucuronoxylans. The action of the enzyme on birchwood acetyl-glucuronoxylan was limited due to the high amount of acetyl substituents. The degree of hydrolysis of partially soluble deacetylated glucuronoxylan did not exceed 50% of the theoretical maximum. However, together with a xylanase hydrolysing the xylan backbone the action of the alpha-glucuronidase of S. commune on glucuronoxylan was clearly enhanced. It was apparent that the enzyme was able to remove the 4-O-methylglucuronic groups mainly from soluble substrates.

Amino Acid Sequence↗
PubMed2003

Linear beta-mannose-containing polysaccharide, beta-xylan, and amylose from the cultured photobiont Trebouxia sp. of the ascolichen Ramalina celastri.

The cultured photobiont Trebouxia sp. of Ramalina celastri was successively extracted at 100 degrees C with hot water, 2% aqueous KOH, and 10% aqueous KOH to give polysaccharide-containing fractions A (2.9%), B (3.9%), and C (0.9% yield) respectively. The intact biont contained 3.8% amylose, which was present in each fraction, and was identified by a blue color formed with iodine solution. In fraction A, and following retrogradation from aqueous solution, it was characterized by (13)C-NMR spectroscopy. Fraction B was treated with alpha-amylase to give a water-soluble fraction consisting mainly of beta-mannose-containing polysaccharides (1.5% yield), whose main component had dn/dc 0.162 and M(r) 17 kDa. Fraction C was subjected to freeze-thawing and the precipitate was treated with alpha-amylase to give a resistant, linear, low molecular mass (1-->4)-linked beta-xylan. The beta-D-mannopyranan preparation contained mainly of 3-O- (28%), 4-O- (11%), and 6-O-substituted Manp units (35%), with 3-O-substituted Rhap units (11%). A controlled Smith degradation provided a beta-mannan with nonreducing end- (8%), 3-O- (85%) and 6-O-substituted units, showing (1-->3)- and (1-->6)-linked structures in the original polysaccharide. These could be present as block-type structures.

Amino Acids↗
PubMed2003

Xylan-hydrolyzing enzyme system from Bacillus pumilus CBMAI 0008 and its effects on Eucalyptus grandis kraft pulp for pulp bleaching improvement.

The extracellular productions of beta-xylanase, beta-xylosidase, beta-glucosidase, beta-mannanase, arabinosidase, alpha-glucuronidase, alpha-galactosidase and Fpase from Bacillus pumilus CBMAI 0008 were investigated with three different xylan sources as substrate. The enzymatic profiles on birchwood, Eucalyptus grandis and oat were studied at alkaline and acidic pH conditions. B. pumilus CBMAI 0008 grown on the three carbon sources produced mainly beta-xylanase. At pH 10, the levels of xylanase were 328, 160 and 136 U/ml, for birch, oat and E. grandis, respectively. beta-Mannanase production was induced on E. grandis (5 U/ml) and arabinofuranosidase on oat (5 U/ml). Although small quantities of alpha-glucuronidase had been produced at pH 10, activity at pH 4.8 was 1.5 U/ml, higher than observed for Aspergillus sp. in literature reports. Preliminary assays carried out on E. grandis kraft pulp from an industrial paper mill (RIPASA S.A. Celulose e Papel, Limeira, SP, Brazil) showed a reduction of 0.3% of chlorine use in the pulp treated with the enzymes, resulting in increased brightness, compared to conventional bleaching. The enzymes were more efficient if applied before the initial bleaching sequence, in a non-pre-oxygenated pulp.

Avena↗
PubMed2002

Site-specific characterization of the association of xylooligosaccharides with the CBM13 lectin-like xylan binding domain from Streptomyces lividans xylanase 10A by NMR spectroscopy.

Endo-beta-1,4-xylanase 10A (Xyn10A) from Streptomyces lividans includes an N-terminal catalytic module and a 130-residue C-terminal family 13 carbohydrate-binding module (CBM13). This latter domain adopts a beta-trefoil structure with three potential binding sites (alpha, beta, and gamma) for a variety of small sugars, xylooligosaccharides, and xylan polymers. To investigate the role of this multivalency in carbohydrate binding, we have used NMR spectroscopy to characterize the interaction of isolated CBM13 with a series of sugars. We have assigned resonances from the main chain nuclei of CBM13 using heteronuclear NMR experiments. Analysis of (15)N NMR relaxation data using the extended model free formalism reveals that CBM13 tumbles as an oblate ellipsoid (D( parallel)/D( perpendicular) = 0.80 +/- 0.02) and that its backbone is relatively rigid on the sub-nanosecond time scale. In particular, the three binding sites show no distinct patterns of increased internal mobility. Ligand-induced chemical shift changes in the (1)H-(15)N HSQC spectra of CBM13 were monitored as a function of increasing concentrations of L-arabinose, lactose, D-xylose, xylobiose, xylotetraose, and xylohexaose. Patterns of shift perturbations for well-resolved resonances demonstrate that all of these sugars associate independently with the three binding sites of CBM13. On the basis of the site-specific association constants derived from a quantitative analysis of these titration data, we show that L-arabinose, lactose, and D-xylose preferentially bind to the alpha site of CBM13, xylobiose binds equally well to all three sites, and xylotetraose and xylohexaose prefer binding to the beta site. Inspection of the crystallographic structure of CBM13 [Notenboom, V., Boraston, A. B., Williams, S. J., Kilburn, D. G., and Rose, D. R. (2002) Biochemistry 41, 4246-4254] provides a rationalization for these results.

Arabinose↗
PubMed2002

The performance of fungal xylan-degrading enzyme preparations in elemental chlorine-free bleaching for Eucalyptus pulp.

Cellulase-free xylan-degrading enzyme preparations from Acrophialophora nainiana, Humicola grisea var. thermoidea and two Trichoderma harzianum strains were used as bleaching agents for Eucalyptus kraft pulp, prior to a chlorine dioxide and alkaline bleaching sequence. In comparison to the control sequence (performed without xylanase pretreatment), the sequence incorporating enzyme treatment was more effective. Removal of residual lignin was indicated by a reduction in kappa number. Overall, enzyme preparations from T. harzianum were marginally more effective in reducing pulp viscosity and chlorine chemical consumption and improving the brightness of the kraft pulp. However, the highest reduction in pulp viscosity was mediated by the xylanase preparation from A. nainiana. Xylanase pretreatment compares very favorably with that of chemical pulping.

Eucalyptus↗
PubMed1997

Isolation and analysis of a gene encoding alpha-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan.

This is the first report describing the analysis of a gene encoding an alpha-glucuronidase, an enzyme essential for the complete breakdown of substituted xylans. A DNA fragment that carries the gene for alpha-glucuronidase was isolated from chromosomal DNA of the hyperthermophilic bacterium Thermotoga maritima MSB8. The alpha-glucuronidase gene (aguA) was identified and characterized with the aid of nucleotide sequence analysis, deletion experiments and expression studies in Escherichia coli, and the start of the coding region was defined by amino-terminal sequencing of the purified recombinant enzyme. The aguA gene encodes a 674-amino-acid, largely hydrophilic polypeptide with a calculated molecular mass of 78593 Da. The alpha-glucuronidase of T. maritima has a novel primary structure with no significant similarity to any other known amino acid sequence. The recombinant enzyme was purified to homogeneity as judged by SDS-PAGE. Gel filtration analysis at low salt concentrations revealed a high apparent molecular mass (> 630 kDa) for the recombinant enzyme, but the oligomeric structure changed upon variation of the ionic strength or the pH, yielding hexameric and/or dimeric forms which were also enzymatically active. The enzyme hydrolysed 2-O-(4-O-methyl-alpha-D-glucopyranosyluronic acid)-D-xylobiose (MeGlcAX2) to xylobiose and 4-O-methylglucuronic acid. The K(m) for MeGlcAX2 was 0.95 mM. The pH optimum was 6.3. Maximum activity was measured at 85 degrees C, about 25 degrees C or more above the values reported for all other alpha-glucuronidases known to date. When incubated at 55-75 degrees C, the enzyme suffered partial inactivation, but thereafter the residual activity remained nearly constant for several days.

Amino Acid Sequence↗
PubMed2000

Thermobacillus xylanilyticus gen. nov., sp. nov., a new aerobic thermophilic xylan-degrading bacterium isolated from farm soil.

An aerobic, thermophilic, xylanolytic, spore-forming bacterium, XETP (T = type strain; P = patent strain), has been isolated from farm soil situated underneath a manure heap in northern France. Strain XETP, which stained negative in the Gram test, occurs as short rods which sometimes form chains. Its spores are ellipsoidal, central to subterminal and occur in swollen sporangia. It grows at temperatures up to 63 degrees C and in the pH range 6.5-8.5. When grown on glucose in optimal conditions, its doubling time was found to be 33 min. CO2 was observed to have a growth-stimulating effect at the start of the culture. In addition to glucose, the isolate utilizes xylose, arabinose, mannose, cellobiose, galactose, maltose, sucrose, xylan and starch. Growth is inhibited by 5% NaCl. The G+C content of strain XETP is 57.5 mol%. The 16S rDNA sequence analysis indicated that strain XETP falls into the radiation of the Bacillus-Lactobacillus-Streptococcus subdivision of the Gram-positive phylum. Its three closest phylogenetic relatives are 'Bacillus viscosus', Paenibacillus curdlanolyticus and Bacillus popilliae with identity values of 91.15, 90.94 and 90.92%, respectively. The major cellular fatty acids are 14-methyl pentadecanoic acid (16:0 iso), hexadecanoic acid (16:0) and 14-methyl hexadecanoic acid (17:0 anteiso). On the basis of 16S rRNA sequence and chemotaxonomic characteristics, the isolate is different enough for it to be considered as a member of a new genus. It is therefore proposed that this isolate represents a new genus and species: Thermobacillus xylanilyticus. Strain XETP, the type strain of Thermobacillus xylanilyticus, has been deposited in the Collection Nationale de Cultures Microbiennes (CNCM I-1017) as a patent strain.

Aerobiosis↗
PubMed2000

Clostridium algidixylanolyticum sp. nov., a psychrotolerant, xylan-degrading, spore-forming bacterium.

A psychrotolerant Clostridium species was isolated from vacuum-packed, temperature-abused raw lamb. Colonies of this micro-organism on sheep-blood agar were circular with an entire margin, grey-white, translucent and beta-haemolytic. Cells were single, tapered, motile rods. Elliptical subterminal spores were produced in the late stationary growth phase. Spores did not cause swelling of the maternal cells. The micro-organism was obligately anaerobic. In peptone yeast extract glucose starch (PYGS) broth at pH 7.0, the micro-organism grew optimally between 25.5 and 30.0 degrees C. The temperature range for growth was 2.5-32.2 degrees C. At 26 degrees C, the micro-organism grew optimally at pH 6.8 to 7.0. The pH range for anaerobic growth was 4.7-9.1. The micro-organism was saccharoclastic, hydrolysed starch and degraded xylan. The fermentation products formed in PYGS broth were acetate, formate, lactate, ethanol, butyrate, butanol, hydrogen and carbon dioxide. The G + C content of the DNA was 38.4 mol%. Phylogenetic analyses indicated that the strain belongs to cluster XIVa of the genus Clostridium (sensu Collins et al. 1994). The new strain differed from phylogenetically related clostridia in terms of cellular fatty acid composition, soluble protein profiles and phenotypic properties. On the basis of phenotypic and genotypic characterization data, the strain was assigned to a new species, namely Clostridium algidixylanolyticum. The type strain is strain SPL73T (= DSM 12273T).

Animals↗
PubMed1995

Genes encoding xylan and beta-glucan hydrolysing enzymes in Bacillus subtilis: characterization, mapping and construction of strains deficient in lichenase, cellulase and xylanase.

The gene encoding extracellular xylanase (xynA) was amplified as a 770 bp DNA fragment from Bacillus subtilis 168 chromosomal DNA by PCR. The genes encoding endo-beta-1,4-glucanase (eglS) and endo-beta-1,3-1,4-glucanase (bglS) were isolated from a genomic library of B. subtilis 168. The sequences of xynA and eglS were identical to those of the xylanase and cellulase genes from B. subtilis PAP115. Integrative plasmids containing DNA fragments with deletions in the coding region of the genes were constructed and used to replace the chromosomal eglS, bglS and xynA genes of B. subtilis 168. Strains without any detectable activity against xylan (Xyn-), carboxymethylcellulose (Egl-) or mixed linked beta-1,3-1,4-glucan (Egl- Bgl-) were obtained. The genes were mapped at 170 degrees (eglS), 175 degrees (xynA) and 340 degrees (bglS) on the B. subtilis chromosome.

Bacillus subtilis↗
PubMed2005

Microbacterium xylanilyticum sp. nov., a xylan-degrading bacterium isolated from a biofilm.

A novel xylan-degrading bacterium, S3-E(T), was isolated from the biofilm of a membrane bioreactor. The cells of this strain were Gram-positive, non-motile, non-spore-forming rods, produced primary branches and formed yellow colonies on nutrient agar. The strain had chemotaxonomic markers that were consistent with classification in the genus Microbacterium, i.e. MK-12, MK-11 and MK-13 as the major menaquinones, predominant iso- and anteiso-branched cellular fatty acids, glucose and galactose as the cell-wall sugars, peptidoglycan-type B2beta with glycolyl residues and a DNA G+C content of 69.7 mol%. Phylogenetic analysis, based on 16S rRNA gene sequencing, showed that strain S3-E(T) is most similar to Microbacterium hominis IFO 15708(T) and Microbacterium foliorum DSM 12966(T) (97.6 and 97.4% sequence similarity, respectively), and that it forms a separate lineage with M. hominis in the genus Microbacterium. DNA-DNA hybridization results and phenotypic properties showed that strain S3-E(T) could be distinguished from all known Microbacterium species and represented a novel species, for which the name Microbacterium xylanilyticum sp. nov. is proposed; the type strain is S3-E(T) (=DSM 16914(T)=KCTC 19079(T)).

Actinomycetales↗
PubMed2005

Use of xylan-rich cost effective agro-residues in the production of xylanase by Streptomyces cyaneus SN32.

AIM: The present study aimed at optimization of cultural and nutritional parameters for enhanced production of xylanase from Streptomyces cyaneus SN32. METHODS AND RESULTS: The xylanase production by S. cyaneus SN32 on most of the agro-residues tested in this study was more, as compared with the xylanase yield in the medium supplemented with commercial xylan. The presence of wheat bran as carbon source in the medium induced the highest production of xylanase followed by corn cob. Utilization of maize stalk, gram husk and black gram husk for microbial xylanase production has been reported first time in the present study. Among all the organic and inorganic sources of nitrogen tested in the study, peptone was found to be the best in stimulating xylanase production by S. cyaneus SN32. CONCLUSION: The production of xylanase from this thermoalkalophilic actinomycete has been enhanced 1.44-fold. To the best of our knowledge, the magnitude of enzyme yield i.e. 720 IU ml(-1) by S. cyaneus SN32 has not been reported for any other actinomycete so far. SIGNIFICANCE AND IMPACT OF STUDY: Present studies revealed that thermoalkalophilic S. cyaneus SN32, because of its simple nutritional requirements and its ability to exhibit considerably good enzyme yield, is a potent xylanase producer for its economical application in various industries.

Agriculture↗
PubMed1980

Inducible beta-xyloside permease as a constituent of the xylan-degrading enzyme system of the yeast Cryptococcus albidus.

The yeast, Cryptococcus albidus, depending on whether it is grown on xylan or glucose, differs remarkably in the ability to take up inducers of extracellular endo-1,4-beta-xylanase synthesis. In washed, glucose-grown cells the initially low ability to take up xylobiose or methyl beta-D-xylopyranoside, increases during incubation with these compounds after a lag-phase shorter than the induction time of the extracellular beta-xylanase. Using of methyl beta-D-[U-14C]xylopyranoside as a very slowly metabolizable inducer of beta-xylanase it has been established that the increase of the rate of xylobiose or methyl xyloside uptake is due to induction of an active transport system for methyl beta-D-xyloside and beta-1,4-xylooligosaccharides. The system is called beta-xyloside permease. The permease activity of induced cells decreases in the absence of beta-xylanase inducers. The induction of permease as well as its inactivation (degradation) can be prevented with cycloheximide, thus both events appear to be dependent on de novo protein synthesis. In analogy with other active transport systems, beta-xyloside permease function can be effectively blocked by inhibitors of energy metabolism in the cells. The demonstrated example of induction of a permease, for inducers and products of hydrolysis of an extracellular polysaccharide hydrolase, points to a new feature of induction of extracellular enzymes in eucaryotic microorganisms.

Biological Transport, Active↗
PubMed2003

Characterization of molecular weight distribution of oligomers from autocatalyzed batch hydrolysis of xylan.

Oat spelt xylan was treated with water in a batch reactor at temperaturesof 180 and 200 degrees C. Ion-moderated partition (IMP) chromatography was thenapplied to separate oligomers in solution according to their molecular size. Calibration of the IMP measurements based on peak height was found toquantify dissolved monomer and oligomer yields well. Oligomer concentrationsin the liquid hydrolysate were also determined from the difference inxylose monomer concentrations measured by high-performance liquid chromatographybefore and after posthydrolysis of dissolved xylooligosaccharidesto xylose. Delayed formation and then rapid disappearance of oligomersfrom DP10 to DP2 was observed by IMP, and total oligomer yields measuredby IMP and posthydrolysis were very similar at these times. However, whileIMP detected virtually no oligomers initially, posthydrolysis measurementsgave significant amounts of soluble oligomers at these times, indicating thatoligomers with chain lengths >10 were in solution but not detectable by theIMP system used.

Avena↗
PubMed2001

Severity function describing the hydrolysis of xylan using carbonic acid.

Beech wood derived xylan to hydrolyzed to predominantly xylose monomer units after exposure to hot, compressed liquid water saturated with carbon dioxide. Similar treatment without CO2 saturation resulted in only minor hydrolysis and a smaller fraction of monomers among the hydrolysis products. Severity of the hydrolysis reaction was correlated to reaction time, temperature, and carbon dioxide partial pressure and followed a function similar to those used to characterize mineral acid systems. Results from parallel hydrolysis experiments with an aqueous system and a very dilute sulfuric acid system allowed an approximation of the dissociation constant of carbonic acid in the temperature range of 170-230 degrees C. Results suggest that carbonic acid may be a viable reagent for promoting hydrolysis without mineral acids, especially in the case of a bioprocessing plant that produces carbon dioxide.

Biomass↗
PubMed1990

Structure of rice-straw arabinoglucuronoxylan and specificity of Streptomyces xylanase toward the xylan.

Rice-straw treated with 5% ammonia water was hydrolyzed with the beta-xylanase of Streptomyces sp. E-86, and four kinds of hetero-oligosaccharides, two arabinoxylo- and two glucuronoxylo-oligosaccharides, were isolated from the hydrolysate by charcoal column, gel filtration, ion-exchange, and aminopropyl silica column chromatographies. The structures of the oligosaccharides were identified as 3(2)-alpha-L-arabinofuranosyl-xylobiose, 3(2)-alpha-L-arabinofuranosylxylotriose, 2(3)-4-O-methyl-alpha-D-glucuronosylxylotriose, and 2(3)-alpha-D-glucuronosylxylotriose by the analysis of component sugar, partial acid hydrolysis, methylation analysis etc. Based on the structures of above oligosaccharides, the structure of rice-straw arabinoglucuronoxylan and the specificity of the xylanase toward the xylan are discussed.

Carbohydrate Conformation↗
PubMed1997

Structure, hormonal regulation, and chromosomal location of genes encoding barley (1-->4)-beta-xylan endohydrolases.

A gene encoding (1-->4)-beta-xylan xylanohydrolase (EC 3.2.1.8) isoenzyme X-I has been isolated from a barley genomic library and the nucleotide sequence of a 2704-bp fragment defined. The gene contains a single intron of 91 bp in the coding region of the mature enzyme and additional introns may be present in the 5'-untranslated region. Expression of the xylanase gene is restricted to the aleurone layer of germinated grain, where the phytohormone gibberellic acid induces both transcriptional activity of the gene and the secretion of active enzyme from the layers. Abscisic acid abolishes the gibberellic acid induction of xylanase gene expression. The hormonal responses are consistent with the presence of promoter sequences, all of which are within 150 bp of the putative transcription start site, that have been implicated as cis-acting elements within gibberellic acid response complexes in plant genes. The elements include a pyrimidine box, CTCTTTCC, together with TAACGAC and TATCCAT boxes. Three genes encode (1-->4)-beta-xylanase isoenzymes in barley and these have been mapped on the barley genome using two doubled haploid populations and seven wheat-barley addition lines. The three xylanase genes are closely linked on the long arm of chromosome 7 (5H). No recombination was detected between the genes in 234 doubled haploid lines. The genes are flanked by the RFLP markers CDO506 on the proximal side and PSR370 at the distal end.

Amino Acid Sequence↗
PubMed1986

Quantitative analysis of a polysulfated xylan (SP54) in urine using gas-liquid chromatography.

A sensitive analytical method for the quantitation of a polysulfated xylan (SP54) in urine has been developed. SP54 and urinary glycosaminoglycans have been isolated from urine using cetylpyridinium chloride. This method removes all glycosaminoglycans with molecular weights less than 3000 Da. Following isolation, SP54 and urinary glycosaminoglycans have been selectively hydrolyzed under conditions (0.5 M HCl/105 degrees C/30 min) which produce an efficient yield of xylose from SP54 but not from the glycosaminoglycans. Xylose derived from SP54 has subsequently been determined using gas-liquid chromatography. Levels of SP54 down to 10 micrograms/ml have been determined using this technique.

Chromatography, Gas↗