Maltohexaose
(Synonyms: 麦芽六糖,Amylohexaose) 目录号 : GC36535
Maltohexaose (Amylohexaose) is a polysaccharide with 6 units of glucose and can be classified as a maltodextrin.
Cas No.:34620-77-4
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Maltohexaose (Amylohexaose) is a polysaccharide with 6 units of glucose and can be classified as a maltodextrin.
| Cas No. | 34620-77-4 | SDF | |
| 别名 | 麦芽六糖,Amylohexaose | ||
| 分子式 | C36H62O31 | 分子量 | 990.86 |
| 溶解度 | Water: 250 mg/mL (252.31 mM) | 储存条件 | Store at -20°C,protect from light |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.0092 mL | 5.0461 mL | 10.0922 mL |
| 5 mM | 0.2018 mL | 1.0092 mL | 2.0184 mL |
| 10 mM | 0.1009 mL | 0.5046 mL | 1.0092 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Maltohexaose-indocyanine green (MH-ICG) for near infrared imaging of endocarditis
PLoS One 2021 Mar 1;16(3):e0247673.PMID:33647027DOI:10.1371/journal.pone.0247673.
Infectious endocarditis is a life-threatening disease, and diagnostics are urgently needed to accurately diagnose this disease especially in the case of prosthetic valve endocarditis. We show here that Maltohexaose conjugated to indocyanine green (MH-ICG) can detect Staphylococcus aureus (S. aureus) infection in a rat model of infective endocarditis. The affinity of MH-ICG to S. aureus was determined and had a Km and Vmax of 5.4 μM and 3.0 X 10-6 μmol/minutes/108 CFU, respectively. MH-ICG had no detectable toxicity to mammalian cells at concentrations as high as 100 μM. The in vivo efficiency of MH-ICG in rats was evaluated using a right heart endocarditis model, and the accumulation of MH-ICG in the bacterial vegetations was 2.5 ± 0.2 times higher than that in the control left ventricular wall. The biological half-life of MH-ICG in healthy rats was 14.0 ± 1.3 minutes, and approximately 50% of injected MH-ICG was excreted into the feces after 24 hours. These data demonstrate that MH-ICG was internalized by bacteria with high specificity and that MH-ICG specifically accumulated in bacterial vegetations in a rat model of endocarditis. These results demonstrate the potential efficacy of this agent in the detection of infective endocarditis.
AmyM, a Novel Maltohexaose-Forming α-Amylase from Corallococcus sp. strain EGB
Appl Environ Microbiol 2015 Mar;81(6):1977-87.PMID:25576603DOI:10.1128/AEM.03934-14.
A novel α-amylase, AmyM, was purified from the culture supernatant of Corallococcus sp. strain EGB. AmyM is a maltohexaose-forming exoamylase with an apparent molecular mass of 43 kDa. Based on the results of matrix-assisted laser desorption ionization-time of flight mass spectrometry and peptide mass fingerprinting of AmyM and by comparison to the genome sequence of Corallococcus coralloides DSM 2259, the AmyM gene was identified and cloned into Escherichia coli. amyM encodes a secretory amylase with a predicted signal peptide of 23 amino acid residues, which showed no significant identity with known and functionally verified amylases. amyM was expressed in E. coli BL21(DE3) cells with a hexahistidine tag. The signal peptide efficiently induced the secretion of mature AmyM in E. coli. Recombinant AmyM (rAmyM) was purified by Ni-nitrilotriacetic acid (NTA) affinity chromatography, with a specific activity of up to 14,000 U/mg. rAmyM was optimally active at 50°C in Tris-HCl buffer (50 mM; pH 7.0) and stable at temperatures of <50°C. rAmyM was stable over a wide range of pH values (from pH 5.0 to 10.0) and highly tolerant to high concentrations of salts, detergents, and various organic solvents. Its activity toward starch was independent of calcium ions. The Km and Vmax of recombinant AmyM for soluble starch were 6.61 mg ml(-1) and 44,301.5 μmol min(-1) mg(-1), respectively. End product analysis showed that Maltohexaose accounted for 59.4% of the maltooligosaccharides produced. These characteristics indicate that AmyM has great potential in industrial applications.
Comparative study on bread quality and starch digestibility of normal and waxy wheat (Triticum aestivum L.) modified by Maltohexaose producing α-amylases
Food Res Int 2022 Dec;162(Pt A):112034.PMID:36461255DOI:10.1016/j.foodres.2022.112034.
It is highly desirable to produce bread with both acceptable texture and health benefits. In this study, Maltohexaose (G6) producing amylase AmyM and its truncation AmyM-TR2 from Corallococcus sp. strain EGB were used to determine their effects to bread quality and starch physicochemical properties. During bread fermentation, AmyM or AmyM-TR2 continuously degraded the starch, resulting in more obvious decrease in relative crystallinity, the ordered structure, pasting viscosities and gelatinization enthalpy of starch than in control. The dough treated with AmyM or AmyM-TR2 increased bread volume and slowly digestible starch content, decreased bread hardness, and extended bread shelf life and as compared with control, and the dough treated with AmyM-TR2 had better improvement effects than AmyM. The volume and slowly digestible starch content of bread from the treatment of AmyM-TR2 increased by 9.74% and 7.56% in normal wheat, 1.42% and 10.28% in waxy wheat as compared with AmyM, respectively. AmyM-TR2 affected the substrate targeting, proximity and structure disruption effects, which contributed to the degradation of more starch than AmyM.
PET imaging of bacterial infections with fluorine-18-labeled Maltohexaose
Angew Chem Int Ed Engl 2014 Dec 15;53(51):14096-14101.PMID:25330976DOI:10.1002/anie.201408533.
A positron emission tomography (PET) tracer composed of (18)F-labeled Maltohexaose (MH(18)F) can image bacteria in vivo with a sensitivity and specificity that are orders of magnitude higher than those of fluorodeoxyglucose ((18)FDG). MH(18)F can detect early-stage infections composed of as few as 10(5) E. coli colony-forming units (CFUs), and can identify drug resistance in bacteria in vivo. MH(18)F has the potential to improve the diagnosis of bacterial infections given its unique combination of high specificity and sensitivity for bacteria.
The action of starch synthase II on 6"'-alpha-maltotriosyl-maltohexaose comprising the branch point of amylopectin
Eur J Biochem 2001 Sep;268(18):4878-84.PMID:11559356DOI:10.1046/j.1432-1327.2001.02413.x.
The principle of using a chemically synthesized, well-defined branched oligosaccharide to provide a more detailed knowledge of the substrate specificity of starch synthase II (SSII) is demonstrated. The branched nonasaccharide, 6"'-alpha-maltotriosyl-maltohexaose, was investigated as a primer for particulate SSII using starch granules prepared from the low-amylose pea mutant lam as the enzyme source. The starch granule preparation from the lam pea mutant contains no starch synthases other than SSII and is devoid of alpha-amylase, beta-amylase and phosphorylase activity. SSII was demonstrated to catalyse a specific nonprocessive elongation of the nonreducing end of the shortest unit chain of 6"'-alpha-maltotriosyl-maltohexaose, i.e. the maltotriose chain. Maltotriose and Maltohexaose, representing the two linear building units of the branched nonasaccharide, were also tested as primers for SSII. Maltotriose was elongated more efficiently than 6"'-alpha-maltotriosyl-maltohexaose and Maltohexaose was used less efficiently. Compared to the surface exposed alpha-glucan chains of the granule bound amylopectin molecules, all three soluble oligosaccharides tested were poor primers for SSII. This indicates that in vivo, the soluble oligosaccharides supposedly released as result of amylopectin trimming reactions are not re-introduced into starch biosynthetic reactions via the action of the granule bound fraction of SSII.