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12 резултати
Relative deposition of xylan and 8-5'-linked lignin structure in Chamaecyparis obtusa, as revealed by double immunolabeling by using monoclonal antibodies.
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CONCLUSIONS
Immunolabeling by using monoclonal antibodies showed that xylan deposition precedes the formation of 8-5'-linked structure of lignin in normal and compression woods of Chamaecyparis obtusa. Xylan deposition and formation of 8-5'-linked lignin structure in differentiating xylems from
Distribution of (1->4)-beta-galactans, arabinogalactan proteins, xylans and (1->3)-beta-glucans in tracheid cell walls of softwoods.
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Polysaccharides were located in the walls of normal and compression wood tracheids of Pinus radiata (radiata pine), Picea sitchensis (Sitka spruce) and Picea abies (Norway spruce) by transmission electron microscopy using immunogold labelling with monoclonal antibodies to (1-->4)-beta-galactan
Occurrence of xylan and mannan polysaccharides and their spatial relationship with other cell wall components in differentiating compression wood tracheids of Cryptomeria japonica.
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Compression wood (CW) tracheids have different cell wall components than normal wood (NW) tracheids. However, temporal and spatial information on cell wall components in CW tracheids is poorly understood. We investigated the distribution of arabino-4-O-methylglucuronoxylans (AGXs) and
Probing the structural basis for the difference in thermostability displayed by family 10 xylanases.
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Thermostability is an important property of industrially significant hydrolytic enzymes: understanding the structural basis for this attribute will underpin the future biotechnological exploitation of these biocatalysts. The Cellvibrio family 10 (GH10) xylanases display considerable sequence
Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.
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TM0077 from Thermotoga maritima is a member of the carbohydrate esterase family 7 and is active on a variety of acetylated compounds, including cephalosporin C. TM0077 esterase activity is confined to short-chain acyl esters (C2-C3), and is optimal around 100°C and pH 7.5. The positional specificity
Structure-function relationships in Gan42B, an intracellular GH42 β-galactosidase from Geobacillus stearothermophilus.
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Geobacillus stearothermophilus T-6 is a Gram-positive thermophilic soil bacterium that contains a battery of degrading enzymes for the utilization of plant cell-wall polysaccharides, including xylan, arabinan and galactan. A 9.4 kb gene cluster has recently been characterized in G.
Structural insights into the specificity of Xyn10B from Paenibacillus barcinonensis and its improved stability by forced protein evolution.
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Paenibacillus barcinonensis is a soil bacterium bearing a complex set of enzymes for xylan degradation, including several secreted enzymes and Xyn10B, one of the few intracellular xylanases reported to date. The crystal structure of Xyn10B has been determined by x-ray analysis. The enzyme folds into
A unique octameric structure of Axe2, an intracellular acetyl-xylooligosaccharide esterase from Geobacillus stearothermophilus.
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Geobacillus stearothermophilus T6 is a thermophilic, Gram-positive soil bacterium that possesses an extensive and highly regulated hemicellulolytic system, allowing the bacterium to efficiently degrade high-molecular-weight polysaccharides such as xylan, arabinan and galactan. As part of the
Structural comparison, docking and substrate interaction study of modeled endo-1, 4-beta xylanase enzyme of Bacillus brevis.
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Xylanase belongs to, Glycoside hydrolase family, playing a major role in xylan degradation. Bacterial and most of the fungal Xylanase, are categorized as true Xylanase belong to GH 10 and GH 11 families. Xylanase is an industrially important enzyme. Most of the research has progressed in the field
Structure-specificity relationships of an intracellular xylanase from Geobacillus stearothermophilus.
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Geobacillus stearothermophilus T-6 is a thermophilic Gram-positive bacterium that produces two selective family 10 xylanases which both take part in the complete degradation and utilization of the xylan polymer. The two xylanases exhibit significantly different substrate specificities. While the
Structural analysis of alpha-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity.
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An alpha-L-arabinofuranosidase (TmAFase) from Thermotoga maritima MSB8 is a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes. In the present study, we carried out the
A pair of esterases from a commensal gut bacterium remove acetylations from all positions on complex β-mannans.
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β-mannans and xylans are important components of the plant cell wall and they are acetylated to be protected from degradation by glycoside hydrolases. β-mannans are widely present in human and animal diets as fiber from leguminous plants and as thickeners and stabilizers in processed foods. There
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