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kojibiose | 2864-54-2

中文名称
——
中文别名
——
英文名称
kojibiose
英文别名
2-alpha-D-glucosyl-D-glucose;(3R,4S,5S,6R)-6-(hydroxymethyl)-3-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxane-2,4,5-triol
kojibiose化学式
CAS
2864-54-2
化学式
C12H22O11
mdl
——
分子量
342.3
InChiKey
HIWPGCMGAMJNRG-CQUJWQHSSA-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

物化性质

  • 沸点:
    700.9±60.0 °C(Predicted)
  • 密度:
    1.76±0.1 g/cm3(Predicted)

计算性质

  • 辛醇/水分配系数(LogP):
    -4.2
  • 重原子数:
    23
  • 可旋转键数:
    4
  • 环数:
    2.0
  • sp3杂化的碳原子比例:
    1.0
  • 拓扑面积:
    190
  • 氢给体数:
    8
  • 氢受体数:
    11

上下游信息

  • 上游原料
    中文名称 英文名称 CAS号 化学式 分子量
  • 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:
    kojibiose 在 Mortierella alliacea YN-15 α-glucosidase 作用下, 以 acetate buffer 为溶剂, 反应 0.5h, 生成 D-葡萄糖
    参考文献:
    名称:
    Purification and Characterization of a Novel Fungal α-Glucosidase fromMortierella alliaceawith High Starch-hydrolytic Activity
    摘要:
    真菌菌株Mortierella alliacea YN-15是一种能利用可溶性淀粉生产花生四烯酸的菌株,尽管其α-淀粉酶活性无法检测到。在此,通过四步柱层析从培养液中纯化出一种负责淀粉水解的α-葡萄糖苷酶。该酶对麦芽糖和其他低聚糖的水解优先性较低,但能将其作为葡萄糖供体进行转葡萄糖基作用,显示出作为真菌α-葡萄糖苷酶的独特底物特异性。纯化的酶由两个分别为61和31 kDa的异亚基组成,它们之间没有通过共价键连接,但在高盐浓度(0.5 M)下稳定地聚集在一起,在凝胶过滤层析中表现出如同一个92 kDa组分的特性。该酶对麦芽糖的水解活性在55°C和pH 5.0-6.0范围内达到最大,并且在存在乙醇的情况下,形成乙基-α-D-葡萄糖苷的转葡萄糖基反应在pH 5.0和温度范围45-50°C时最优。
    DOI:
    10.1271/bbb.66.2415
  • 作为产物:
    参考文献:
    名称:
    瓜尔豆中三萜皂苷的分离及结构解析
    摘要:
    摘要 从蓝藻籽粕甲醇提取物中分离得到一种新的皂苷,其结构为 3-O-{[α- L -rhamnopyranosyl(1 → 2)]-[α- L -rhamnopyranosyl(1 → 4)]-β- D-吡喃葡萄糖基(1 → 2)-
    DOI:
    10.1016/s0031-9422(00)84540-9
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文献信息

  • Glucoamylase Originating from<i>Schwanniomyces occidentalis</i>Is a Typical α-Glucosidase
    作者:Fumiaki SATO、Masayuki OKUYAMA、Hiroyuki NAKAI、Haruhide MORI、Atsuo KIMURA、Seiya CHIBA
    DOI:10.1271/bbb.69.1905
    日期:2005.1
    A starch-hydrolyzing enzyme from Schwanniomyces occidentalis has been reported to be a novel glucoamylase, but there is no conclusive proof that it is glucoamylase. An enzyme having the hydrolytic activity toward soluble starch was purified from a strain of S. occidentalis. The enzyme showed high catalytic efficiency (kcat⁄Km) for maltooligosaccharides, compared with that for soluble starch. The product anomer was α-glucose, differing from glucoamylase as a β-glucose producing enzyme. These findings are striking characteristics of α-glucosidase. The DNA encoding the enzyme was cloned and sequenced. The primary structure deduced from the nucleotide sequence was highly similar to mold, plant, and mammalian α-glucosidases of α-glucosidase family II and other glucoside hydrolase family 31 enzymes, and the two regions involved in the catalytic reaction of α-glucosidases were conserved. These were no similarities to the so-called glucoamylases. It was concluded that the enzyme and also S. occidentalis glucoamylase, had been already reported, were typical α-glucosidases, and not glucoamylase.
    来自西方施瓦尼霉的淀粉解酶被报道为一种新型的葡萄糖淀粉酶,但尚无确凿证据表明其为葡萄糖淀粉酶。从一种西方施瓦尼霉株中分离出一种对可溶性淀粉具有解活性的酶。与对可溶性淀粉的活性相比,该酶对麦芽低聚糖表现出高催化效率(kcat⁄Km)。产物的异形体为α-葡萄糖,与能产生β-葡萄糖葡萄糖淀粉酶不同。这些发现是α-葡萄糖苷酶的显著特征。编码该酶的DNA被克隆并测序。从核苷酸序列推导出的一级结构与真菌、植物和哺乳动物的α-葡萄糖苷酶II族及其他糖苷解酶家族31的α-葡萄糖苷酶高度相似,并且与α-葡萄糖苷酶催化反应相关的两个区域是保守的。与所谓的葡萄糖淀粉酶并无相似之处。最终得出的结论是,该酶以及已经报道的西方施瓦尼霉的葡萄糖淀粉酶都是典型的α-葡萄糖苷酶,而不是葡萄糖淀粉酶
  • Purification and Characterization of a New Type of α-Glucosidase from<i>Paecilomyces lilacinus</i>That Has Transglucosylation Activity to Produce α-1,3- and α-1,2-Linked…
    作者:Isao KOBAYASHI、Masahiro TOKUDA、Hiroyuki HASHIMOTO、Takashi KONDA、Hirofumi NAKANO、Sumio KITAHATA
    DOI:10.1271/bbb.67.29
    日期:2003.1
    A fungus producing an α-glucosidase that synthesizes α-1,3- and α-1,2-linked glucooligosaccharides by transglucosylation was isolated and identified as Paecilomyces lilacinus. The cell-bound enzyme responsible for the synthesis was extracted by suspension of mycelia with 0.1 M phosphate buffer (pH 8.0), and the extract was purified. The molecular weight and the isoelectric point were estimated to be 54,000 and 9.1, respectively. The enzyme was most active at pH 5.0 and 65°C. The enzyme hydrolyzed maltose, nigerose, and kojibiose. The enzyme also hydrolyzed soluble starch and amylose with the rate toward maltose. p-Nitrophenyl α-glucoside and isomaltose were not good substrates. The enzyme had high transglucosylation activity to synthesize oligosaccharides containing α-1,3- and α-1,2-linkages. At an early stage of the reaction, considerable maltotriose, 4-O-α-nigerosyl-D-glucose, and 4-O-α-kojibiosyl-D-glucose were synthesized. Afterwards, nigerose and kojibiose were accumulated gradually with glucose as an acceptor.
    一种产生α-葡萄糖苷酶的真菌被分离并鉴定为紫色土胞霉(Paecilomyces lilacinus)。负责合成的细胞结合酶通过将菌丝体悬浮于0.1 M磷酸盐缓冲液(pH 8.0)中提取,并对提取物进行了纯化。估计其分子量和等电点分别为54,000和9.1。该酶在pH 5.0和65°C下最为活跃。该酶麦芽糖、黑麦芽糖异麦芽糖。该酶还以与麦芽糖相同的速率可溶性淀粉直链淀粉。对对硝基苯基α-葡萄糖苷和异麦芽糖的底物活性较低。该酶具有较高的转葡萄糖基化活性,可以合成含有α-1,3-和α-1,2-连接的寡糖。在反应早期,合成了相当数量的麦芽三糖、4-O-α-黑麦芽糖基-D-葡萄糖和4-O-α-异麦芽糖基-D-葡萄糖。随后,黑麦芽糖异麦芽糖葡萄糖作为受体逐渐积累。
  • Purification and characterization of an α-glucosidase from germinating millet seeds
    作者:Yoshiki Yamasaki、Mikio Fujimoto、Junji Kariya、Haruyoshi Konno
    DOI:10.1016/j.phytochem.2005.02.024
    日期:2005.4
    4-fold lower than that for maltose. The enzyme preferably hydrolyzed amylopectin in starch, but also readily hydrolyzed nigerose, which has an α-1,3-glucosidic linkage and exists as an abnormal linkage in the structure of starch. In particular, the enzyme readily hydrolyzed millet starch from germinating seeds that had been degraded to some extent.
    摘要 α-葡萄糖苷酶(α-d-葡萄糖葡萄糖解酶,EC 3.2.1.20)通过硫酸分馏、CM-cellulofine/Fractogel EMD SO 3 色谱法从发芽的小米(Panicum miliaceum L.)种子中分离出来。 Sephacryl S-200 HR 和 TSK 凝胶 Phenyl-5 PW,以及制备等电聚焦。该酶通过 SDS-PAGE 是同质的。根据其在 SDS-PAGE 中的迁移率估计该酶的分子量为 86,000,根据 TSKgel super SW 3000 的凝胶过滤估计为 80,000,这表明它由单个单元组成。该酶的等电点为8.3。该酶容易麦芽糖、麦芽低聚糖和 α-1,4-葡聚糖,但多糖的速度比麦芽糖快。K m 值随着底物分子量的增加而降低。麦芽七糖的值比麦芽糖的值低约 4 倍。该酶优选解淀粉中的支链淀粉,但也容易解具有α-1,3-糖苷键且在
  • [EN] A SUCROSE PHOSPHORYLASE FOR THE PRODUCTION OF KOJIBIOSE<br/>[FR] SACCHAROSE PHOSPHORYLASE POUR LA PRODUCTION DE KOJIBIOSE
    申请人:UNIV GENT
    公开号:WO2016075219A1
    公开(公告)日:2016-05-19
    The present invention relates to the production of the disaccharide kojibiose which is known to be a powerful prebiotic. The invention indeed discloses the generation of genetically modified sucrose phosphorylases which convert -via a transglycosylation reaction- sucrose into kojibiose in a very efficient manner. Hence, the present invention relates to a cost-effective production method of kojibiose which is useful within industry.
    本发明涉及生产已知为强效益生元的二糖曲碱的方法。该发明确实揭示了通过转糖基反应将蔗糖高效转化为曲碱的基因修饰蔗糖磷酸化酶的生成。因此,本发明涉及一种在工业中有用的经济高效的曲碱生产方法。
  • Synthesis of sterically crowded derivatives of anomeric pairs of d-glucose disaccharides
    作者:Sanford Mendonca、Roger A. Laine
    DOI:10.1016/j.carres.2005.05.016
    日期:2005.9
    Derivatization of carbohydrates is of considerable interest since the derivatives can be used for structural studies in the field of mass spectrometry. We report here the synthesis of a series of sterically crowded derivatives of various linkage and stereo-isomeric glucose-glucose disaccharides with the impetus being to understand the effect of these derivatized groups on fragmentation of the glycosidic
    碳水化合物的衍生化具有相当大的意义,因为该衍生物可用于质谱领域的结构研究。我们在这里报告了一系列各种键和立体异构体葡萄糖-葡萄糖二糖的空间拥挤衍生物的合成,其推动力是了解这些衍生基团对糖苷键断裂的影响以及用于识别糖基键的方法的发展。异头配置。已经合成了全烷基化的(甲基,乙基,丙基,丁基和戊基),过酸酯化的(乙酰基,新戊酰基,甲基磺酰基)和全甲硅烷基化的(叔丁基-二甲基甲硅烷基)葡萄糖-葡萄糖二糖衍生物。报告。
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