6-kestose | 562-68-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 6-kestose
• 英文别名: (2R,3R,4S,5S,6R)-2-[(2S,3S,4S,5R)-5-[[(2R,3S,4S,5R)-3,4-dihydroxy-2,5-bis(hydroxymethyl)oxolan-2-yl]oxymethyl]-3,4-dihydroxy-2-(hydroxymethyl)oxolan-2-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 562-68-5
• 化学式: C₁₈H₃₂O₁₆
• 分子量: 504.442
• InChiKey: ODEHMIGXGLNAKK-OESPXIITSA-N

物化性质

• 熔点：
  145 °C
• 沸点：
  902.9±65.0 °C(Predicted)
• 密度：
  1.82±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -5.5
• 重原子数：
  34
• 可旋转键数：
  9
• 环数：
  3.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  269
• 氢给体数：
  11
• 氢受体数：
  16

反应信息

• 作为反应物：
  描述：

  氢氟酸 、 6-kestose 生成 D-古洛糖
  参考文献：
  名称：

  BOUCHU, ALAIN;CHEDIN, JEAN;DEFAYE, JACQUES;LAFONT, DIDIER;WONG, EMILE

  摘要：

  DOI：
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 在 enzyme-substances from aerobacter levanium 作用下， 生成 6-kestose
  参考文献：
  名称：

  Feingold et al., Biochemical Journal, 1956, vol. 64, p. 351,353, 357

  摘要：

  DOI：

文献信息

• Molecular insight into regioselectivity of transfructosylation catalyzed by GH68 levansucrase and β-fructofuranosidase
  作者：Masayuki Okuyama、Ryo Serizawa、Masanari Tanuma、Asako Kikuchi、Juri Sadahiro、Takayoshi Tagami、Weeranuch Lang、Atsuo Kimura

  DOI：10.1016/j.jbc.2021.100398

  日期：2021.1

  Glycoside hydrolase family 68 (GH68) enzymes catalyze β-fructosyltransfer from sucrose to another sucrose, the so-called transfructosylation. Although regioselectivity of transfructosylation is divergent in GH68 enzymes, there is insufficient information available on the structural factor(s) involved in the selectivity. Here, we found two GH68 enzymes, β-fructofuranosidase (FFZm) and levansucrase (LSZm)

  糖苷水解酶家族 68 (GH68) 酶催化 β-果糖基从蔗糖转移到另一种蔗糖，即所谓的转果糖基化。尽管转果糖基化的区域选择性在 GH68 酶中有所不同，但关于选择性中涉及的结构因素的信息不足。在这里，我们发现两种 GH68 酶，β-呋喃果糖苷酶 (FFZm) 和果聚糖蔗糖酶 (LSZm)，在运动发酵单胞菌基因组中串联编码，表现出不同的选择性：FFZm 催化 β-(2→1)-转果糖基化 (1-TF) ，而 LSZm 进行 1-TF 和 β-(2→6)-转果糖基化 (6-TF)。我们分别将 His79FFZm 和 Ala343FFZm 及其相应的 Asn84LSZm 和 Ser345LSZm 确定为这些区域选择性的结构因素。LSZm 分别用 FFZm 型 His 和 Ala 替代其 Asn84LSZm 和 Ser345LSZm (N84H/S345A-LSZm) 失去了 6-TF 并增强了 1
• Structural and Kinetic Insights Reveal That the Amino Acid Pair Gln-228/Asn-254 Modulates the Transfructosylating Specificity of Schwanniomyces occidentalis β-Fructofuranosidase, an Enzyme That Produces Prebiotics
  作者：Miguel Álvaro-Benito、M. Angela Sainz-Polo、David González-Pérez、Beatriz González、Francisco J. Plou、María Fernández-Lobato、Julia Sanz-Aparicio

  DOI：10.1074/jbc.m112.355503

  日期：2012.6

  Schwanniomyces occidentalis beta-fructofuranosidase (Ffase) is a GH32 dimeric enzyme that releases fructose from the nonreducing end of various oligosaccharides and essential storage fructans such as inulin. It also catalyzes the transfer of a fructosyl unit to an acceptor producing 6-kestose and 1-kestose, prebiotics that stimulate the growth of bacteria beneficial for human health. We report here

  Schwanniomyces occidentalis β-呋喃果糖苷酶 (Ffase) 是一种 GH32 二聚酶，可从各种寡糖和必需储存果聚糖（如菊粉）的非还原端释放果糖。它还催化果糖基单元向受体的转移，产生 6-kestose 和 1-kestose，这是一种益生元，可刺激有益于人类健康的细菌的生长。我们在此报告了与果糖基麦芽糖和菊粉复合的灭活 Ffase 的晶体结构，这显示了复杂的相互作用网络，使底物紧密结合在活性位点。观察到多达五个亚位点，位于亚位点 +3 的糖单元通过与二聚体中相邻亚基的 β 夹心结构域的相互作用而被识别。这解释了对长底物观察到的高活性，给出了 GH32 β 夹心结构域在底物结合中的直接作用的第一个实验证据。关键残基发生突变，它们的水解酶/转移酶 (H/T) 活性得到充分表征，表明 Gln-228/Asn-254 对参与调节 H/T 比和 β(2-1)/β 型(2
• Formation of trisaccharides (kestoses) by pyrolysis of sucrose
  作者：Merilyn Manley-Harris、Geoffrey N. Richards

  DOI：10.1016/0008-6215(91)89045-h

  日期：1991.10

  Amorphous sucrose, containing citric acid as catalyst, undergoes thermolysis at 100 degrees to yield fructofuranosyl cation and D-glucose. The cation reacts with unchanged sucrose to form all three of the known kestoses, and also their alpha-fructofuranosyl anomers. Two of the latter are resistant to invertase hydrolysis. A new fructosylglucose disaccharide is also formed.

  含有柠檬酸作为催化剂的无定形蔗糖在100度进行热解，生成果糖呋喃糖基阳离子和D-葡萄糖。阳离子与未改变的蔗糖反应形成所有三种已知的蔗糖，以及它们的α-果糖呋喃糖基异构体。后者中的两个抗转化酶水解。还形成了新的果糖基葡萄糖二糖。
• Invertase-catalysed fructosyl transfer in concentrated solutions of sucrose
  作者：Adrie J.J. Straathof、Antonius P.G. Kieboom、Herman van Bekkum

  DOI：10.1016/0008-6215(86)85033-9

  日期：1986.1
• Optimization of levansucrase/endo-inulinase bi-enzymatic system for the production of fructooligosaccharides and oligolevans from sucrose
  作者：Feng Tian、Maryam Khodadadi、Salwa Karboune

  DOI：10.1016/j.molcatb.2014.08.005

  日期：2014.11

  A bi-enzymatic system based on the combined use of levansucrase (LS) from Bacillus amyloliquefaciens and endo-inulinase from Aspergillus niger in a one-step reaction was investigated for the synthesis of fructooligosaccharides (FOSs) and oligolevans using sucrose as the sole substrate. Sucrose concentration was the most important independent variable, whilst LS to endo-inulinase ratio exhibited significant effects on the end-product profiles. The interaction between sucrose concentration and reaction time exhibited significant effect on all responses. At the initial stage of time course, short chain FOSs (scFOSs, 1-kestose, nystose, 1(F)-fructosylnystose) were the major products, whilst 6-kestose, medium chain fructooligosaccharides (mcFOSs, levanohexaose, levanopentaose) and oligolevans became the dominant ones at the late stage. The optimal conditions leading to a high yield of scFOSs (1:1 ratio, 0.5 h, 0.6 M) were different from those resulting in a high yield of mcFOSs and oligolevans (1.85:1 ratio, 1.77 h, 0.6 M). The bi-enzymatic system has a great potential for the production of FOSs and oligolevans at a large scale because of its high yield (57-65%, w/w) and productivity (65.8-266.8 g/L h), and its uses of low temperature (35 degrees C) and low concentration of sucrose. To the best of our knowledge, this is the first study on the optimization of a LS/endo-inulinase bi-enzymatic system. (C) 2014 Elsevier B.V. All rights reserved.