麦芽糖基海藻糖 | 25545-20-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 麦芽糖基海藻糖
• 中文别名: alpha-D-吡喃葡萄糖基O-alpha-D-吡喃葡萄糖基-(1→4)-O-alpha-D-吡喃葡萄糖基-(1→4)-alpha-D-吡喃葡萄糖苷
• 英文名称: maltosyltrehalose
• 英文别名: O-α-D-glucopyranosyl-(1->4)-O-α-D-glucopyranosyl-(1->4)-O-α-D-glucopyranosyl-α-D-glucopyranoside；Maltosyl trehalose；(2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 25545-20-4
• 化学式: C₂₄H₄₂O₂₁
• 分子量: 666.585
• InChiKey: CTEMZTQLPNKNKP-REGJXUDFSA-N

物化性质

• 沸点：
  1036.3±65.0 °C(Predicted)
• 密度：
  1.83±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -8.5
• 重原子数：
  45
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  348
• 氢给体数：
  14
• 氢受体数：
  21

反应信息

• 作为反应物：
  描述：

  麦芽糖基海藻糖 在 citrate-phosphate buffer 作用下， 生成 麦芽糖 、 海藻糖
  参考文献：
  名称：

  嗜热古细菌Sulfolobus solfataricus ATCC 35092中的麦芽寡糖基海藻糖海藻糖水解酶的表达，纯化和鉴定。

  摘要：

  麦芽寡糖基海藻糖海藻糖水解酶（MTHase）主要在麦芽寡糖基海藻糖的α-1,1-连接的末端二糖旁边切割α-1,4-葡糖苷键，以产生海藻糖和较低分子量的麦芽寡糖。在这项研究中，编码MTHase的treZ基因从Sulfolobus solfataricus ATCC 35092中被PCR克隆，然后在大肠杆菌中表达。在没有IPTG诱导的情况下，获得了高产量的活性野生型MTHase（13300单位/克湿细胞）。使用热处理，核酸沉淀和离子交换色谱法依次纯化野生型MTHase。纯化的野生型MTHase的最适pH值为5，最适温度为85℃。该酶在3.5到11的pH值范围内稳定。并且在45-85摄氏度下孵育2小时后，活性得以完全保留。水解度为（DP）4-7的麦芽寡糖基海藻糖水解酶的k（cat）值为193、1030、1190和分别为1230 s（-1），而DP 4-7麦芽低聚糖水解过程中葡萄糖形成的k（cat）值分别为5

  DOI：

  10.1021/jf061318z
• 作为产物：
  描述：

  maltotetraose 在 maltooligosyltrehalose synthase F₄₀₅M mutant 作用下， 以 various solvent(s) 为溶剂， 生成 麦芽糖基海藻糖
  参考文献：
  名称：

  Protein Engineering of Sulfolobus solfataricus Maltooligosyltrehalose Synthase To Alter Its Selectivity

  摘要：

  Maltooligosyltrehalose synthase (MTSase) is one of the key enzymes involved in trehalose production from starch and catalyzes an intramolecular transglycosylation reaction by converting the alpha-1,4- to alpha,alpha-1,1-glucosidic linkage. Mutations at residues F206, F207, and F405 were constructed to change the selectivity of the enzyme because the changes in selectivity could reduce the side hydrolysis reaction of releasing glucose and thus increase trehalose production from starch. As compared with wild-type MTSase, F405Y and F405M MTSases had decreased ratios of the initial rate of glucose formation to that of trehalose formation in starch digestion at 75 degrees C when wild-type and mutant MTSases were, respectively, used with isoamylase and maltooligosyltrehalose trehalohydrolase (MTHase). The highest trehalose yield from starch digestion was by the mutant MTSase having the lowest initial rate of glucose formation to trehalose formation, and this predicted high trehalose yield better than the ratio of catalytic efficiency for hydrolysis to that for transglycosylation.

  DOI：

  10.1021/jf0701279

文献信息

• Formation of Trehalose from Maltooligosaccharides by a Novel Enzymatic System
  作者：Kazuhiko Maruta、Tetsuya Nakada、Michio Kubota、Hiroto Chaen、Toshiyuki Sugimoto、Masashi Kurimoto、Yoshio Tsujisaka

  DOI：10.1271/bbb.59.1829

  日期：1995.1

  A trehalose-producing bacterium, Arthrobacter sp. strain Q36, was isolated from soil. From a supernatant of the culture broth, two novel enzymes related to trehalose synthesis were partially purified by Sepabeads FP-DA column chromatography. One enzyme catalyzed the conversion of maltopentaose into maltotriosyl trehalose by intramolecular transglycosylation, showing it to be maltooligosyl trehalose synthase. The other hydrolyzed the product transferred by the former into maltotriose and trehalose specifically, showing it to be maltooligosyl trehalose trehalohydrolase. In addition to the bacterial strain isolated, several bacteria kept in our laboratory were found to produce these enzymes. The enzymatic system was proposed to be a novel biosynthesis of trehalose in bacteria involving the following reactions: maltodextrin→maltooligosyl trehalose, maltooligosyl trehalose→maltodextrin + trehalose. When these enzymes acted on amylose simultaneously, the trehalose in the reaction mixture reached more than 80% in content.

  从土壤中分离出了一种产生曲哈糖的细菌--节杆菌 Q36 菌株。通过 Sepabeads FP-DA 柱色谱法，从培养液的上清液中部分纯化出两种与三卤糖合成有关的新型酶。一种酶通过分子内转糖基化催化麦芽酮戊糖转化为麦芽三糖，表明它是麦芽寡糖三糖合成酶。另一种则将前者转移的产物特异性地水解为麦芽三糖和曲哈糖，表明它是麦芽寡糖基曲哈糖曲哈水解酶。除了分离出的细菌菌株外，我们还发现实验室中的几种细菌也能产生这些酶。该酶系统被认为是细菌中一种新型的三卤糖生物合成方法，涉及以下反应：麦芽糊精→麦芽寡糖基三卤糖，麦芽寡糖基三卤糖→麦芽糊精+三卤糖。当这些酶同时作用于直链淀粉时，反应混合物中的三卤糖含量达到 80% 以上。
• Synthesis of Glycosyl-trehaloses by Cyclomaltodextrin Glucanotransferase through the Transglycosylation Reaction
  作者：Masashi Kurimoto、Akihiko Tabuchi、Takahiko Mandai、Takashi Shibuya、Hiroto Chaen、Shigeharu Fukuda、Toshiyuki Sugimoto、Yoshio Tsujisaka

  DOI：10.1271/bbb.61.1146

  日期：1997.1

  Cyclomaltodextrin glucanotransferase from Bacillus stearothermophilus produced a series of glycosyl-trehaloses through the transglycosylation reaction with cyclomaltohexaose as the glycosyl donor and trehalose as its acceptor. After β-amylase treatment, five species of glycosyl-trehaloses were isolated by column chromatography. After chemical and enzymatic analyses, it was concluded that these oligosaccharides were α-maltosyl α-d-glucopyranoside, α-maltotriosyl α-d-glucopyranoside, α-maltosyl α-maltoside, α-maltotriosyl α-maltoside, and α-maltotriosyl α-maltotrioside. These were not hydrolyzed by salivary amylase, artificial gastric juice, or pancreatic amylase, however they were hydrolyzed by enzymes of the small intestine.

  嗜热脂肪芽孢杆菌的环麦芽糊精葡聚糖转移酶以环己糖为糖基供体，以曲哈糖为受体，通过转糖基化反应产生了一系列糖基曲哈糖。经过β-淀粉酶处理后，通过柱层析分离出了五种糖基-曲哈糖。经过化学和酶学分析，这些低聚糖分别是 α-麦芽糖基 α-d-吡喃葡萄糖苷、α-麦芽三糖基 α-d-吡喃葡萄糖苷、α-麦芽糖基 α-麦芽糖苷、α-麦芽三糖基 α-麦芽糖苷和 α-麦芽三糖基 α-麦芽三糖苷。这些物质不会被唾液淀粉酶、人工胃液或胰淀粉酶水解，但会被小肠酶水解。
• All-α-d-linked tetra- and penta-saccharide substructures of Trestatin A by block syntheses with triflic anhydride as promoter
  作者：Hans Peter Wessel、Beatrice Mayer、Gerhard Englert

  DOI：10.1016/0008-6215(93)80028-d

  日期：1993.4

  The perbenzylated maltosyl and maltotriosyl fluorides 6 and 16 were treated with 2,3,2',3',6'-penta-O-benzyl-4,6-O-benzylidene-alpha,alpha-trehalose (7) using triflic anhydride as a promoter to give all-alpha-D-linked tetra- and penta-saccharides which were finally deblocked to the free oligosaccharides 4-O-alpha-maltosyl- 9 and 4-O-alpha-maltotriosyl-alpha,alpha-trehaloses 18. The H-1 NMR spectra of some of the compounds were fully analyzed by 1D TOCSY and ROESY experiments.
• Mutations on Aromatic Residues of the Active Site To Alter Selectivity of the<i> Sulfolobus solfataricus</i> Maltooligosyltrehalose Synthase
  作者：Tsuei-Yun Fang、Wen-Chi Tseng、Yao-Te Chung、Ching-Hsing Pan

  DOI：10.1021/jf060152z

  日期：2006.5.1

  Mutations Y290F, Y367F, F405Y, and Y409F located near subsite + 1 were constructed in maltooligosyltrehalose synthase (MTSase) to alter the selectivity of the enzyme. These mutations were designed to evaluate the effects of hydrophobic interactions and/or hydrogen bondings on transglycosylation and side hydrolysis reactions. The catalytic efficiencies of Y290F MTSase for hydrolysis and transglycosylation reactions were only 6.6 and 5.6%, respectively, of those of wildtype MTSase, whereas the catalytic efficiencies of Y367F MTSase were decreased by about half. F405Y MTSase had similar catalytic efficiencies for transglycosylation and a somewhat lower catalytic efficiency for hydrolysis. Y409F MTSase had somewhat lower catalytic efficiencies for the transglycosylation and a similar catalytic efficiency for hydrolysis. Y290F and Y367F MTSases had large changes in (G), suggesting that there are hydrogen bonds between the substrate and residues Y290 and Y367 of wild-type MTSase. Compared with wild-type MTSase, F405Y MTSase had decreased ratios of hydrolysis to transglycosylation, whereas Y290F, Y367F, and Y409F MTSases had increased ratios. These results suggest that use of F405Y MTSase might result in a higher yield of trehalose production from starch when it replaces wild-type MTSase.