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β-xylopentaose | 83009-08-9

中文名称
——
中文别名
——
英文名称
β-xylopentaose
英文别名
xylopentaose;Xyl(b1-4)Xyl(b1-4)Xyl(b1-4)Xyl(b1-4)b-Xyl;(2S,3R,4S,5R)-2-[(3R,4R,5R,6S)-6-[(3R,4R,5R,6S)-6-[(3R,4R,5R,6S)-4,5-dihydroxy-6-[(3R,4R,5R,6R)-4,5,6-trihydroxyoxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxyoxan-3-yl]oxy-4,5-dihydroxyoxan-3-yl]oxyoxane-3,4,5-triol
β-xylopentaose化学式
CAS
83009-08-9
化学式
C25H42O21
mdl
——
分子量
678.596
InChiKey
LFFQNKFIEIYIKL-KUFDKHFESA-N
BEILSTEIN
——
EINECS
——
  • 物化性质
  • 计算性质
  • ADMET
  • 安全信息
  • SDS
  • 制备方法与用途
  • 上下游信息
  • 反应信息
  • 文献信息
  • 表征谱图
  • 同类化合物
  • 相关功能分类
  • 相关结构分类

计算性质

  • 辛醇/水分配系数(LogP):
    -8.6
  • 重原子数:
    46
  • 可旋转键数:
    8
  • 环数:
    5.0
  • sp3杂化的碳原子比例:
    1.0
  • 拓扑面积:
    326
  • 氢给体数:
    12
  • 氢受体数:
    21

上下游信息

  • 下游产品
    中文名称 英文名称 CAS号 化学式 分子量

反应信息

  • 作为反应物:
    描述:
    β-xylopentaose 在 endo-1,4-β-D-xylanase from Sporotrichum thermophile 作用下, 以 acidic aq. solution 为溶剂, 反应 1.0h, 以49%的产率得到D-(+)-xylobiose
    参考文献:
    名称:
    Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile
    摘要:
    An endo-beta-1,4-xylanase (1,4-beta-D-xylan xylanoxydrolase, EC 3.2.1.8) present in culture filtrates of Sporotrichum thermophile ATCC 34628 was purified to homogeneity by Q-Sepharose Lind Sephacryl S-200 column chromatographies. The enzyme has a molecular mass of 25,000 Da, an isoelectric point of 6.7, and is optimally active at pH 5 and at 70 degreesC. Thin-layer chromatography (TLC) analysis showed that endo-xylanase liberates mainly xylose (Xyl) and xylobiose (Xyl,) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methylglucuronoxylan and rhodymenan (a beta-(1-->4)-beta(1-->3)-xylan). Also, the enzyme releases an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. Analysis of reaction mixtures by high performance liquid chromatography (HPLC) revealed that the enzyme cleaves preferentially the internal glycosidic bonds of xylooligosaccharides, [1-H-3]-xylooligosaccharides and xylan. The enzyme also hydrolyses the 4-methylumbelliferyl glycosides of beta-xylobiose and beta-xylotriose at the second glycosidic bond adjacent to the aglycon. The endoxylanase is not active on pNPX and pNPC. The enzyme mediates a decrease in the viscosity of xylan associated with a release of only small amounts of reducing sugar. The enzyme is irreversibly inhibited by series of omega-epoxyalkyl glycosides of D-Xylopyranose. The results suggest that the endoxylanase from S. thermophile has catalytic properties similar to the enzymes belonging to family 11. (C) 2003 Elsevier Ltd. All rights reserved.
    DOI:
    10.1016/s0008-6215(03)00291-x
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文献信息

  • Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile
    作者:Petros Katapodis、Maria Vršanská、Dimitris Kekos、Wim Nerinckx、Peter Biely、Marc Claeyssens、Basil J Macris、Paul Christakopoulos
    DOI:10.1016/s0008-6215(03)00291-x
    日期:2003.9
    An endo-beta-1,4-xylanase (1,4-beta-D-xylan xylanoxydrolase, EC 3.2.1.8) present in culture filtrates of Sporotrichum thermophile ATCC 34628 was purified to homogeneity by Q-Sepharose Lind Sephacryl S-200 column chromatographies. The enzyme has a molecular mass of 25,000 Da, an isoelectric point of 6.7, and is optimally active at pH 5 and at 70 degreesC. Thin-layer chromatography (TLC) analysis showed that endo-xylanase liberates mainly xylose (Xyl) and xylobiose (Xyl,) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methylglucuronoxylan and rhodymenan (a beta-(1-->4)-beta(1-->3)-xylan). Also, the enzyme releases an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. Analysis of reaction mixtures by high performance liquid chromatography (HPLC) revealed that the enzyme cleaves preferentially the internal glycosidic bonds of xylooligosaccharides, [1-H-3]-xylooligosaccharides and xylan. The enzyme also hydrolyses the 4-methylumbelliferyl glycosides of beta-xylobiose and beta-xylotriose at the second glycosidic bond adjacent to the aglycon. The endoxylanase is not active on pNPX and pNPC. The enzyme mediates a decrease in the viscosity of xylan associated with a release of only small amounts of reducing sugar. The enzyme is irreversibly inhibited by series of omega-epoxyalkyl glycosides of D-Xylopyranose. The results suggest that the endoxylanase from S. thermophile has catalytic properties similar to the enzymes belonging to family 11. (C) 2003 Elsevier Ltd. All rights reserved.
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