xylobiose

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: xylobiose
• 英文别名: Xylopyranosyl-(1-4)-d-xylopyranose；(3R,4S,5R)-2-[(3R,4R,5R)-4,5,6-trihydroxyoxan-3-yl]oxyoxane-3,4,5-triol
• 化学式: C₁₀H₁₈O₉
• 分子量: 282.248
• InChiKey: LGQKSQQRKHFMLI-GZNHDWAXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4
• 重原子数：
  19
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  149
• 氢给体数：
  6
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  xylobiose 在 xylanase XYN IV from trichoderma reesei 作用下， 以 aq. buffer 为溶剂， 生成 D-吡喃木糖
  参考文献：
  名称：

  Xylanase XYN IV fromTrichoderma reeseishowing exo- and endo-xylanase activity

  摘要：

  A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA‐2Xyl‐4Xyl‐4Xyl, HexA3Xyl3), releasing the reducing‐end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo‐β‐1,4‐xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan‐hydrolyzing endo‐β‐1,4‐glucanase EG I. XYN IV was able to degrade several different β‐1,4‐xylans, but was inactive on β‐1,4‐mannans and β‐1,4‐glucans. It showed both exo‐and endo‐xylanase activity. Rhodymenan, a linear soluble β‐1,3‐β‐1,4‐xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β‐xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4‐O‐methyl‐d‐glucuronic acid (MeGlcA) substituents as substrate specificity determinants.

  DOI：

  10.1111/febs.12069
• 作为产物：
  描述：

  methyl β-D-xylobioside 在 xylanase XYN IV from trichoderma reesei 作用下， 以 aq. buffer 为溶剂， 生成 xylobiose
  参考文献：
  名称：

  Xylanase XYN IV fromTrichoderma reeseishowing exo- and endo-xylanase activity

  摘要：

  A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA‐2Xyl‐4Xyl‐4Xyl, HexA3Xyl3), releasing the reducing‐end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo‐β‐1,4‐xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan‐hydrolyzing endo‐β‐1,4‐glucanase EG I. XYN IV was able to degrade several different β‐1,4‐xylans, but was inactive on β‐1,4‐mannans and β‐1,4‐glucans. It showed both exo‐and endo‐xylanase activity. Rhodymenan, a linear soluble β‐1,3‐β‐1,4‐xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β‐xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4‐O‐methyl‐d‐glucuronic acid (MeGlcA) substituents as substrate specificity determinants.

  DOI：

  10.1111/febs.12069

文献信息

• Development of a multifunctional neoglycoside auxiliary for applications in glycomics research
  作者：Thamrongsak Cheewawisuttichai、Matthew Brichacek

  DOI：10.1039/d1ob00941a

  日期：——

  A novel, multifunctional, tetrazine-containing neoglycoside auxiliary has been synthesized in three steps and 28% overall yield.

  一种新型、多功能、含四嗪基团的新糖苷辅助剂已经在三个步骤中合成，总产率为28%。
• The enhancement of xylose monomer and xylotriose degradation by inorganic salts in aqueous solutions at 180 °C
  作者：Chaogang Liu、Charles E. Wyman

  DOI：10.1016/j.carres.2006.07.017

  日期：2006.11

  The inorganic salts KCl, NaG, CaCl2, MgCl2, and FeCl3, and especially the latter, significantly increased xylose monomer and xylotriose degradation in water heated to 180 degrees C with unaccountable losses of xylose amounting to as high as 65% and 78% for xylose and xylotriose, respectively, after 20 min incubation with 0.8% FeCl3. Furthermore, losses of both xylose and xylotriose were well described by first order homogeneous kinetics, and the rate constants for xylose and xylotriose disappearance increased 6-and 49-fold, respectively, when treated with 0.8% FeCl3 solution compared to treatment with just pressurized hot water at the same temperature. Although the addition of these inorganic salts produced a significant drop in pH, the degradation rates with salts were much faster than could be accounted for by a pH change. For example, the rate constants for the disappearance of xylose and xylotriose with 0.8% FeCl3 were 3-fold and 7-fold greater, respectively, than for treatment with very dilute sulfuric acid at the same pH. In addition, xylose losses were greater than could be accounted for by just furfural production, suggesting that other degradation products were also formed, and xylose losses to unidentified compounds increased significantly with the addition of FeCl3. The unidentified compounds could be formed through aqueous furfural resinification and condensation reactions that are accelerated by FeCl3, but the actual mechanisms are still not clear. (c) 2006 Published by Elsevier Ltd.
• Structure of an arabinoxylan from the bark of Persea macrantha (Lauraceae)
  作者：D.Channe Gowda、J.Pape Gowda、Yernool V. Anjaneyalu

  DOI：10.1016/s0008-6215(00)81796-6

  日期：1982.10
• Xylanase XYN IV from<i>Trichoderma reesei</i>showing exo- and endo-xylanase activity
  作者：Maija Tenkanen、Mária Vršanská、Matti Siika-aho、Dominic W. Wong、Vladimír Puchart、Merja Penttilä、Markku Saloheimo、Peter Biely

  DOI：10.1111/febs.12069

  日期：2013.1

  A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA‐2Xyl‐4Xyl‐4Xyl, HexA3Xyl3), releasing the reducing‐end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo‐β‐1,4‐xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan‐hydrolyzing endo‐β‐1,4‐glucanase EG I. XYN IV was able to degrade several different β‐1,4‐xylans, but was inactive on β‐1,4‐mannans and β‐1,4‐glucans. It showed both exo‐and endo‐xylanase activity. Rhodymenan, a linear soluble β‐1,3‐β‐1,4‐xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β‐xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4‐O‐methyl‐d‐glucuronic acid (MeGlcA) substituents as substrate specificity determinants.