best substrate, TLC analysis of CtXynGH30 hydrolysis products from beechwood xylan. CtXynGH30 shows the release of a series of higher xylooligosaccharides, overview
acts predominantly on polysaccharides with xylan as the main chain and substituted with varying amounts of glucuronic acids, such as in beechwood xylan, birchwood xylan and 4-O-methylglucuronoxylan
CtXynGH30 shows the release of a series of higher xylooligosaccharides, implying the endo-acting cleavageby the enzyme. No activity on 4-nitrophenyl-beta-D-xylopyranoside indicating that CtXynGH30 lacks exo-cleaving activity. No activity with carob galactomannan, galactan (lupin), beta-D-glucan (barley), carboxy methylcellulose, pecticgalactan (apple), pecticgalactan (Citrus), pecticgalactan (lupin), rhamnogalacturonan, curdlan, pullulan, and pustulan
the enzyme does not present activity against arabinan, oat spelt xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-L-arabinopyranoside, and 4-nitrophenyl alpha L-arabinopyranoside
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant crystallized in complex with xylohexaose, by the hanging-drop vapour-phase diffusion method, to beyond 2.0 A resolution. Crystals belong to space group P3221 and contain a dimer in the asymmetric unit
structure of a truncated derivative of comprising exclusively the enzyme catalytic module. The enzyme displays a (beta/alpha)8 TIM-barrel core with a side-associated beta-sheet domain. In mutant E225A, solved in the presence of xylotetraose, xylotetraose-cleavage oligosaccharides partially occupy subsites -3 to +2. The sugar ring at the +1 subsite is held in place by hydrophobic stacking interactions between Tyr139 and Tyr200 and hydrogen bonds to the OH group of Tyr227. The xylopyranosyl ring at the -1 subsite appears in the alpha-anomeric configuration
generation of two constructs of XynC, one with its cellulose binding domain and the catalytic domain, pXynC-BC, and the other with only the catalytic domain, pXynC-C. The specific activities of XynC with and without the non-catalytic domains are similar
generation of two constructs of XynC, one with its cellulose binding domain and the catalytic domain, pXynC-BC, and the other with only the catalytic domain, pXynC-C. The specific activities of XynC with and without the non-catalytic domains are similar
generation of two constructs of XynZ: pXynZ-BDC, which includes the dockerin domain, and pXynZ-C, which does not. For XynZ, the specific activity of the enzyme without the non-catalytic domains is about 5fold greater than that of the intact enzyme. The overall increase in activity is 9fold higher for XynZ-C versus XynZ-BDC
generation of two constructs of XynZ: pXynZ-BDC, which includes the dockerin domain, and pXynZ-C, which does not. For XynZ, the specific activity of the enzyme without the non-catalytic domains is about 5fold greater than that of the intact enzyme. The overall increase in activity is 9fold higher for XynZ-C versus XynZ-BDC
during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C
Conservation in the mechanism of glucuronoxylan hydrolysis revealed by the structure of glucuronoxylan xylanohydrolase (CtXyn30A) from Clostridium thermocellum
A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans
A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans