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At least 289 records · Page 16Linked to original sources
PubMed1983

Arabinan synthase and xylan synthase activities of Phaseolus vulgaris. Subcellular localization and possible mechanism of action.

Membrane fractions from bean hypocotyl or suspension cultures incorporated arabinose from UDP-beta-L-arabinose into arabinan and xylose from UDP-alpha-D-xylose in vitro; the level of each activity was dependent on the state of differentiation of the cells. These activities may be due to single transglycosylases, since no lipid or proteinaceous intermediate acceptors were found in either case. Subcellular fractionation studies showed that enzyme activity in vitro was localized in both Golgi-derived membranes and endoplasmic reticulum in similar amounts. However, incorporation into the polymers in vivo in suspension culture cells incubated with [1-3H]arabinose was considerably greater in the Golgi-derived membranes. Thus, although these enzymes may be translated and inserted at the level of the endoplasmic reticulum, their activities are under other levels of control, so that most of the activity in vivo is confined to the Golgi apparatus. Initiation of glycosylation in the endoplasmic activity may, however, occur.

Arabinose↗
PubMed2004

Inhibition of 1,4-beta-D-xylan xylanohydrolase by the specific aspartic protease inhibitor pepstatin: probing the two-step inhibition mechanism.

This is the first report that describes the inhibition mechanism of xylanase from Thermomonospora sp. by pepstatin A, a specific inhibitor toward aspartic proteases. The kinetic analysis revealed competitive inhibition of xylanase by pepstatin A with an IC50 value 3.6 +/- 0.5 microm. The progress curves were time-depended, consistent with a two-step slow tight binding inhibition. The inhibition followed a rapid equilibrium step to form a reversible enzyme-inhibitor complex (EI), which isomerizes to the second enzyme-inhibitor complex (EI*), which dissociated at a very slow rate. The rate constants determined for the isomerization of EI to EI* and the dissociation of EI* were 15 +/- 1 x 10(-5) and 3.0 +/- 1 x 10(-8) s(-1), respectively. The Ki value for the formation of EI complex was 1.5 +/- 0.5 microm, whereas the overall inhibition constant Ki* was 28.0 +/- 1 nm. The conformational changes induced in Xyl I by pepstatin A were monitored by fluorescence spectroscopy, and the rate constants derived were in agreement with the kinetic data. Thus, the conformational alterations were correlated to the isomerization of EI to EI*. Pepstatin A binds to the active site of the enzyme and disturbs the native interaction between the histidine and lysine, as demonstrated by the abolished isoindole fluorescence of o-phthalaldehyde-labeled xylanase. Our results revealed that the inactivation of xylanase is due to the interference in the electronic microenvironment and disruption of the hydrogen-bonding network between the essential histidine and other residues involved in catalysis, and a model depicting the probable interaction between pepstatin A with xylanase has been proposed.

Actinobacteria↗
PubMed1987

Structure and expression of genes coding for xylan-degrading enzymes of Bacillus pumilus.

The complete nucleotide sequence of the beta-xylosidase gene (xynB) of Bacillus pumilus IPO and its flanking regions was established. A 1617-bp open reading frame for beta-xylosidase, a homodimer enzyme, was observed. The amino acid sequence of the N-terminal region and the molecular mass 62607 Da) of the beta-xylosidase subunit, deduced from the DNA sequence, agreed with the result obtained with the purified enzyme. The Shine-Dalgarno sequence was found 8 bp upstream of the initiation codon, ATG. The xylanase gene (xynA) of the same strain was 4.6 kbp downstream of the 3' end of xynB, and its DNA sequence was reported in our previous paper [Fukusaki, E., Panbangred, W., Shinmyo, A. & Okada, H. (1984) FEBS Lett. 171, 197-201]. The results of the Northern hybridization suggested that the mRNA of xynA and xynB were produced separately. The 5' and 3' ends of the xynA and xynB gene were mapped with nuclease S1. The '-10' regions for promoter sequences of both genes were similar to the consensus sequence for B. subtilis RNA polymerases, the '-35' regions were different from all the known promoters for B. subtilis RNA polymerases.

Amino Acid Sequence↗
PubMed1995

Purification and Characterization of the (alpha)-Glucuronidase from Thermoanaerobacterium sp. Strain JW/SL-YS485, an Important Enzyme for the Utilization of Substituted Xylans.

A cell-associated (alpha)-glucuronidase was purified to gel electrophoretic homogeneity from the thermophilic anaerobic bacterium Thermoanaerobacterium sp. strain JW/SL-YS485. This enzyme had a pI of 4.65, a molecular weight of 130,000, and two subunits; the molecular weight of each subunit was 74,000. The enzyme exhibited the highest level of activity at pH 5.4 and 60(deg)C, as determined by a 5-min assay. The K(infm) and k(infcat) values of the enzyme for 4-methylglucuronosyl xylobiose were 0.76 mM and 1,083 IU/(mu)mol, respectively. The Arrhenius energy was 26.4 kJ/mol. The specific activities of the enzyme with 4-O-methylglucuronosyl xylobiose, 4-O-methylglucuronosyl xylotriose, and 4-O-methylglucuronosyl xylotetraose were 8.4, 4.8, and 3.9 IU/mg, respectively. The purified (alpha)-glucuronidase and a (beta)-xylosidase purified from the same organism interacted synergistically to hydrolyze 4-methylglucuronosyl xylotetraose.

Journal Article↗
PubMed2002

Evidence for temporal regulation of the two Pseudomonas cellulosa xylanases belonging to glycoside hydrolase family 11.

Pseudomonas cellulosa is a highly efficient xylan-degrading bacterium. Genes encoding five xylanases, and several accessory enzymes, which remove the various side chains that decorate the xylan backbone, have been isolated from the pseudomonad and characterized. The xylanase genes consist of xyn10A, xyn10B, xyn10C, xyn10D, and xyn11A, which encode Xyn10A, Xyn10B, Xyn10C, Xyn10D, and Xyn11A, respectively. In this study a sixth xylanase gene, xyn11B, was isolated which encodes a 357-residue modular enzyme, designated Xyn11B, comprising a glycoside hydrolase family 11 catalytic domain appended to a C-terminal X-14 module, a homologue of which binds to xylan. Localization studies showed that the two xylanases with glycoside hydrolase family (GH) 11 catalytic modules, Xyn11A and Xyn11B, are secreted into the culture medium, whereas Xyn10C is membrane bound. xyn10C, xyn10D, xyn11A, and xyn11B were all abundantly expressed when the bacterium was cultured on xylan or beta-glucan but not on medium containing mannan, whereas glucose repressed transcription of these genes. Although all of the xylanase genes were induced by the same polysaccharides, temporal regulation of xyn11A and xyn11B was apparent on xylan-containing media. Transcription of xyn11A occurred earlier than transcription of xyn11B, which is consistent with the predicted mode of action of the encoded enzymes. Xyn11A, but not Xyn11B, exhibits xylan esterase activity, and the removal of acetate side chains is required for xylanases to hydrolyze the xylan backbone. A transposon mutant of P. cellulosa in which xyn11A and xyn11B were inactive displayed greatly reduced extracellular but normal cell-associated xylanase activity, and its growth rate on medium containing xylan was indistinguishable from wild-type P. cellulosa. Based on the data presented here, we propose a model for xylan degradation by P. cellulosa in which the GH11 enzymes convert decorated xylans into substituted xylooligosaccharides, which are then hydrolyzed to their constituent sugars by the combined action of cell-associated GH10 xylanases and side chain-cleaving enzymes.

Acetates↗
PubMed1985

Xylanolytic Activity of Clostridium acetobutylicum.

Of 20 strains of Clostridium spp. screened, 17 hydrolyzed larch wood xylan. Two strains of Clostridium acetobutylicum, NRRL B527 and ATCC 824, hydrolyzed xylan but failed to grow on solid media with larch xylan as the sole carbon source; however, strain ATCC 824 was subsequently found to grow on xylan under specified conditions in a chemostat. These two strains possessed cellulolytic activity and were therefore selected for further studies. In cellobiose-limited continuous cultures, strain NRRL B527 produced maximum xylanase activity at pH 5.2. Strain ATCC 824 produced higher xylanase, xylopyranosidase, and arabinofuranosidase activities in chemostat culture with xylose than with any other soluble carbon source as the limiting nutrient. The activities of these enzymes were markedly reduced when the cells were grown in the presence of excess glucose. The xylanase showed maximum activity at pH 5.8 to 6.0 and 65 degrees C. The enzyme was stable on the alkaline side of pH 5.2 but was unstable below this pH value. The extracellular xylanolytic activity from strain ATCC 824 hydrolyzed 12% of the larch wood xylan during a 24-h incubation period, yielding xylose, xylobiose, and xylotriose as the major hydrolysis products. Strain ATCC 824, after being induced to grow in batch culture in xylan medium supplemented with a low concentration of xylose, failed to grow reproducibly in unsupplemented xylan medium. A mutant obtained by mutagenesis with ethyl methanesulfonate was able to grow reproducibly in batch culture on xylan. Both the parent strain and the mutant were able to grow with xylan as the sole source of carbohydrate in continuous culture with the pH maintained at either 5.2 or 6.0. Under these conditions, the cells utilized approximately 50% of the xylan.

Journal Article↗
PubMed2002

A comparison of liquid hot water and steam pretreatments of sugar cane bagasse for bioconversion to ethanol.

Sugar cane bagasse was pretreated with either liquid hot water (LHW) or steam using the same 25 l reactor. Solids concentration ranged from 1% to 8% for LHW pretreatment and was > or = 50% for steam pretreatment. Reaction temperature and time ranged from 170 to 230 degrees C and 1 to 46 min, respectively. Key performance metrics included fiber reactivity, xylan recovery, and the extent to which pretreatment hydrolyzate inhibited glucose fermentation. In four cases, LHW pretreatment achieved > or = 80% conversion by simultaneous saccharification and fermentation (SSF). > or = 80% xylan recovery, and no hydrolyzate inhibition of glucose fermentation yield. Combined effectiveness was not as good for steam pretreatment due to low xylan recovery. SSF conversion increased and xylan recovery decreased as xylan dissolution increased for both modes. SSF conversion, xylan dissolution. hydrolyzate furfural concentration, and hydrolyzate inhibition increased, while xylan recovery and hydrolyzate pH decreased, as a function of increasing LHW pretreatment solids concentration (1-8%). These results are consistent with the notion that autohydrolysis plays an important. if not exclusive, role in batch hydrothermal pretreatment. Achieving concurrently high (greater than 90%) SSF conversion and xylan recovery will likely require a modified reactor configuration (e.g. continuous percolation or base addition) that better preserves dissolved xylan.

Biodegradation, Environmental↗
PubMed1997

Stability and chemical modification of xylanase from Aspergillus sp. (2M1 strain).

The 2M1 strain of Aspergillus sp., which showed high extracellular xylanolytic activities in a pre-screening, was studied. Oat-spelt, birch, eucalyptus and pine xylans were used as xylanolytic inductors. The following activities were found at 50 degrees C in the presence of 1% xylan: 120 units/ml (oat-spelt xylan), 132 units/ml (birch xylan), 107 units/ml (eucalyptus xylan), 67 units/ml (pine xylan) and 137 units/ml (larch-wood xylan). Xylanase induced by pine xylan exhibited a higher stability than those induced by the other xylans. The stability was improved by addition of glycerol. In the crude extract, reagents which were found to affect xylanase activity were 1-ethyl-3-(3-dimethylaminopropyl)carbodi-imide for amidation of carboxylic groups and N-bromosuccinimide at a concentration of 0.5 mM for indole oxidation. Methylene Blue, butane-2,3-dione, N-acetylimidazole, chloramine-T and iodoacetate had little effect on the enzyme activity (more than 97% of the original activity remained).

Aspergillus↗