Isomaltotriose
(Synonyms: 异麦芽三糖) 目录号 : GC38802
Isomaltotriose 是由 Leuconostoc mesenteroides NRRL B-512 中的葡萄糖经酶解得到的一种糖。
Cas No.:3371-50-4
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
Isomaltotriose is a sugar from enzymic hydrolyzates of the dextran from Leuconostoc mesenteroides NRRL B-512[1].
[1]. ALLENE JEANES, et al. Isomaltose and Isomaltotriose from Enzymic Hydrolyzates of Dextran.
| Cas No. | 3371-50-4 | SDF | |
| 别名 | 异麦芽三糖 | ||
| Canonical SMILES | O=C[C@@H]([C@H]([C@@H]([C@@H](CO[C@@H]1[C@@H]([C@H]([C@@H]([C@@H](CO[C@@H]2[C@@H]([C@H]([C@@H]([C@@H](CO)O2)O)O)O)O1)O)O)O)O)O)O)O | ||
| 分子式 | C18H32O16 | 分子量 | 504.44 |
| 溶解度 | Water: ≥ 250 mg/mL (495.60 mM) | 储存条件 | Store at -20°C |
| 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 | 1.9824 mL | 9.912 mL | 19.824 mL |
| 5 mM | 0.3965 mL | 1.9824 mL | 3.9648 mL |
| 10 mM | 0.1982 mL | 0.9912 mL | 1.9824 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。
Enzymatic synthesis of Isomaltotriose palmitate and evaluation of its emulsifying property
Enzyme Microb Technol 2017 Jun;101:51-56.PMID:28433191DOI:10.1016/j.enzmictec.2017.03.004.
Enzymatic syntheses of oligosaccharide fatty acid esters are important owing to their wide range of industrial applications in the food, cosmetic, and pharmaceutical industries. Transesterification of Isomaltotriose and palmitic acid vinyl ester, catalyzed by the metalloprotease thermolysin, was performed in organic solvents. The process parameters (reaction time and temperature) were optimized to achieve the highest yield of Isomaltotriose palmitate (IP). The water content of the reaction system played a key role in the acylation of Isomaltotriose. Dimethyl sulfoxide was thought to be the most suitable reaction medium by taking the degree of substitution of the modified Isomaltotriose into account. The optimum reaction time, temperature, water content, and enzyme concentration were 24h, 45°C, 40%, and 0.05%, respectively, under which the product yield was as high as 89.7%. The enzyme operational stability study showed that thermolysin retained 51.5% of its initial activity for the synthesis of IP (even after repeated use for 72h). Moreover, test results showed that the emulsifying capacity and emulsion stability of IP are 107.5mL oil/g ester and 16.3%, respectively.
Purification and characterization of an isomaltotriose-producing endo-dextranase from a Fusarium sp
Biosci Biotechnol Biochem 1998 Jan;62(1):117-22.PMID:9501522DOI:10.1271/bbb.62.117.
An isomaltotriose-producing endo-dextranase was simply purified from cell-free culture broth of a Fusarium sp. by ethanol fractionation and consecutive column chromatographies using DEAE-Toyopearl and Bio-Gel P-100. The purified enzyme was judged to be homogeneous on PAGE and SDS-PAGE as well as isoelectric focusing. The molecular mass of the enzyme was estimated to be about 69 kDa by SDS-PAGE. The enzyme is an acidic protein with a pI of 4.6. The optimum pH and temperature were pH 6.5 and 35 degrees C, respectively. The enzyme was completely stable over the range of pH 4.5-11.8 at 4 degrees C for 24 h and at temperatures below 45 degrees C. Inactivation of the enzyme was found to be partial with 5 mM Cu2+, being about 70% inhibition and complete with 5 mM of Fe3+, Hg2+, Ag+ or NBS. The enzyme split dextran in an endo-lytic action to produce a large amount of Isomaltotriose and a slight amount of isomaltose and glucose. The anomeric configurations of the reaction products formed by the enzyme were alpha-form, indicating that the alpha-glycoside linkages in the substrate are retained. The final yield of Isomaltotriose from dextran T-2000 was about 62%.
The action pattern of Penicillium lilacinum dextranase
Carbohydr Res 1975 Feb;39(2):303-15.PMID:1139551DOI:10.1016/s0008-6215(00)86140-6.
The product distributions resulting from the action of Penicillium lilacinum dextranase on end-labelled oligosaccharides of the isomaltose series have been determined. The initial rates of formation of labelled products were measured for Isomaltotriose up to isomalto-octaose, and the molar proportions and radioactivity of the final products from Isomaltotriose up to isomaltohexaose were determined. D-Glucose was released only from Isomaltotriose and isomaltotetraose, by hydrolysis of the first linkage from the reducing end (linkage 1); the terminal bonds of higher members of the series were not attacked. All oligosaccharides except Isomaltotriose were hydrolyzed at more than one linkage. The main points of attack on isomaltotetraose up to isomalto-octaose were at linkage 2, and at the third linkage from the non-reducing end; these two positions coincide for isomaltopentaose. The degradation of Isomaltotriose up to isomalto-octaose was entirely hydrolytic. The enzyme also catalyzed an extremely slow, concentration-dependent degradation of isomaltose, and this may have occurred via a condensation to isomaltotetraose, followed by hydrolysis of linkage 1 to give D-glucose and Isomaltotriose.
Distinguishing Carbohydrate Isomers with Rapid Hydrogen/Deuterium Exchange-Mass Spectrometry
J Am Soc Mass Spectrom 2021 Jan 6;32(1):152-156.PMID:33124815DOI:10.1021/jasms.0c00314.
Carbohydrates play key roles in facilitating cellular functions, yet characterizing their structures is analytically challenging due to the presence of epimers, regioisomers, and stereoisomers. In-electrospray-hydrogen/deuterium exchange-mass spectrometry (in-ESI HDX-MS) is a rapid HDX method that samples solvated carbohydrates with minimal instrument modification. When applied to proteins, HDX is often measured after multiple time points to sample the dynamics of structures. Herein, we alter the HDX reaction time by modifying the spray-solvent conductivity, which changes the initial size of ESI droplets, and thus, the droplet lifetimes. We show that this change in droplet lifetime alters the magnitude of HDX for carbohydrate-metal adducts. Furthermore, we illustrate how monitoring HDX at multiple time points enables three trisaccharide isomers (melezitose, maltotriose, and Isomaltotriose) to be distinguished. This work illustrates the feasibility of this method for characterizing solvated carbohydrates, including isomeric species which differ only by linkage.
In vitro digestibility of commercial and experimental isomalto-oligosaccharides
Food Res Int 2020 Aug;134:109250.PMID:32517953DOI:10.1016/j.foodres.2020.109250.
Isomalto-oligosaccharides (IMO) significantly contribute to the global oligosaccharide market. IMO are linear α-(1 → 6) linked oligosaccharides with Isomaltotriose as the representative trisaccharide. Commercial IMO preparations ypically also contain panose-series oligosaccharides as a major component. In humans, IMO are partially digestible but the digestibility of specific components of commerical IMO preparations remains unknown. This study aimed to compare the in vitro digestibility of reference compounds, experimental α-gluco-oligosaccharides and commercial IMO. Experimental α-gluco-oligosaccharides were synthesized with the recombinant dextransucrase DsrM. Two in vitro digestion methods were used, a reference method matching the AOAC method for dietary fibre, and a protocol that uses brush border glycosyl hydrolases from the rat intestine. The α-gluco-oligosaccharides patterns after hydrolysis remain were analyzed by high performance anion exchange chromatography coupled to pulsed amperometric detection. Panose-series oligosaccharides were hydrolysed more rapidly by amylase and amyloglucosidase when compared to hydrolysis by rat intestinal enzymes. The rate of hydrolysis by rat intestinal enzymes decreased in the order panose > isomaltose, kojibiose or nigerose. Hydrolysis of panose-series oligosaccharides but not the hydrolysis of isomalto-oligosaccharides was dependent on the degree of polymerization. Qualitative analysis of oligosaccharides remaining after hydrolysis indicated that rat small intestinal enzymes hydrolyse their substrates from the non-reducing end. Taken together, results inform on the modification or optimization of current production processes for IMO to obtain tailored oligosaccharide preparations with reduced digestibility and an increased content of dietary fibre.