Allitol
(Synonyms: 蒜糖醇,Allodulcitol) 目录号 : GC64444
Allitol (Allodulcitol) is a rare polyol found in nature that is useful not only as a sweetener, but also as the raw material for production of chemical compounds.
Cas No.:488-44-8
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
Allitol (Allodulcitol) is a rare polyol found in nature that is useful not only as a sweetener, but also as the raw material for production of chemical compounds.
| Cas No. | 488-44-8 | SDF | Download SDF |
| 别名 | 蒜糖醇,Allodulcitol | ||
| 分子式 | C6H14O6 | 分子量 | 182.17 |
| 溶解度 | DMSO : 50 mg/mL (274.47 mM; Need ultrasonic) | 储存条件 | 4°C, away from moisture and 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 | 5.4894 mL | 27.4469 mL | 54.8938 mL |
| 5 mM | 1.0979 mL | 5.4894 mL | 10.9788 mL |
| 10 mM | 0.5489 mL | 2.7447 mL | 5.4894 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。
Effects of Dietary Allitol on Body Fat Accumulation in Rats
J Nutr Sci Vitaminol (Tokyo) 2022;68(4):348-352.PMID:36047107DOI:10.3177/jnsv.68.348.
Allitol is a rare sugar alcohol obtained by reducing d-allulose (d-psicose). However, information on the effects of long-term dietary Allitol intake is limited. This study aimed to investigate the effect of Allitol supplementation, as a sugar substitute, on body fat accumulation in rats compared with sucrose, rare sugar d-allulose, or erythritol. Thirty-two male Wistar rats (3 wk old) were fed experimental diets including 5% sucrose, Allitol, erythritol, or d-allulose for 8 wk ad libitum. Weight gain, food intake, and food efficiency did not differ among the groups. The total body fat mass and percentage, and intra-abdominal adipose tissue weights were significantly lower in rats fed with the Allitol diet than in those fed with the sucrose diet. These body fat indicators tended to be lower in rats fed with the erythritol and d-allulose diets than in those fed with the sucrose diet, but there was no significant difference. The serum glucose-lowering effect obtained in rats fed with the d-allulose diet did not appear in rats fed with the Allitol diet. These results suggest that the anti-obesity effect of Allitol may be equal to or greater than that of d-allulose.
Efficient Allitol Bioproduction from D-Fructose Catalyzed by Recombinant E. coli Whole Cells, and the Condition Optimization, Product Purification
Appl Biochem Biotechnol 2020 Oct;192(2):680-697.PMID:32519252DOI:10.1007/s12010-020-03359-x.
Allitol is a kind of rare sugar alcohol with potential application value. An engineered strain, which simultaneously expressed D-psicose-3-epimerase (DPE), ribitol dehydrogenase (RDH), and formate dehydrogenase (FDH) three enzymes, was constructed by cloning above three genes into one plasmid and transformed into the host E. coli strain, and used as the whole-cell catalysts for biotransformation of Allitol from the low-cost substrate of D-fructose. The whole cell Allitol biotransformation conditions were optimized. The medium, recombinant gene induction conditions, and the substrate feeding rate for cultivation of the catalytic cells were optimized. Then, the fed-batch culture was made and scaled up to 10 L fermentor. Finally, 63.44 g/L Allitol was obtained from 100 g/L D-fructose after 3 h of biotransformation, and the Allitol crystals of 99.9% purity were obtained by using cooling recrystallization. The Allitol production method developed in this research has high product purity, and is highly efficient, easily scaled up, and suitable for large-scale production of highly purified Allitol.
Optimization for Allitol production from D-glucose by using immobilized glucose isomerase and recombinant E. coli expressing D-psicose-3-epimerase, ribitol dehydrogenase and formate dehydrogenase
Biotechnol Lett 2020 Nov;42(11):2135-2145.PMID:32451803DOI:10.1007/s10529-020-02917-x.
Objective: To develop a method combining enzymatic catalysis and resting-cell biotransformation to produce Allitol from low cost substrate D-glucose. Results: The recombinant E. coli expressing D-psicose-3-epimerase (DPE), ribitol dehydrogenase (RDH) and formate dehydrogenase (FDH) for Allitol production from D-fructose was constructed. The optimizations of the cell catalytic conditions and the cell cultivation conditions were made. Then, 63.4 g Allitol L-1 was obtained from 100 g D-fructose L-1 in 4 h catalyzed by the recombinant E. coli cells. In order to decrease the substrate cost, D-glucose was used as the substrate instead of D-fructose and immobilized glucose isomerase was used to convert D-glucose into D-fructose. In order to simplify Allitol production process from D-glucose, one-pot reaction using the mixed catalysts was used and the reaction conditions were optimized. Finally, 12.7 g Allitol L-1 was obtained from 50 g D-glucose L-1 catalyzed by the mixed catalysts of immobilized glucose isomerase and the recombinant E. coli cells. Conclusions: Allitol can be efficiently produced from low cost substrate D-glucose by using the method combining enzymatic catalysis and resting-cell biotransformation, which is the first report.
D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
Front Microbiol 2022 Apr 25;13:870168.PMID:35547110DOI:10.3389/fmicb.2022.870168.
The NAD(P)-dependent alcohol dehydrogenase (ADH) gene was cloned from Gluconobacter frateurii NBRC 3264 and expressed in Escherichia coli BL21 star (DE3). The expressed enzyme was purified and the characteristics were investigated. The results showed that this ADH can convert Allitol into D-allulose (D-psicose), which is the first reported enzyme with this catalytic ability. The optimum temperature and pH of this enzyme were 50°C and pH 7.0, respectively, and the enzyme showed a maximal activity in the presence of Co2+. At 1 mM Co2+ and Allitol concentrations of 50, 150, and 250 mM, the D-allulose yields of 97, 56, and 38%, respectively, were obtained after reaction for 4 h under optimal conditions, which were much higher than that obtained by using the epimerase method of about 30%.
Reconstruction of a Cofactor Self-Sufficient Whole-Cell Biocatalyst System for Efficient Biosynthesis of Allitol from d-Glucose
J Agric Food Chem 2022 Mar 30;70(12):3775-3784.PMID:35298165DOI:10.1021/acs.jafc.2c00440.
The combined catalysis of glucose isomerase (GI), d-psicose 3-epimerase (DPEase), ribitol dehydrogenase (RDH), and formate dehydrogenase (FDH) provides a convenient route for the biosynthesis of Allitol from d-glucose; however, the low catalytic efficiency restricts its industrial applications. Here, the supplementation of 0.32 g/L NAD+ significantly promoted the cell catalytic activity by 1.18-fold, suggesting that the insufficient intracellular NAD(H) content was a limiting factor in Allitol production. Glucose dehydrogenase (GDH) with 18.13-fold higher activity than FDH was used for reconstructing a cofactor self-sufficient system, which was combined with the overexpression of the rate-limiting genes involved in NAD+ salvage metabolic flow to expand the available intracellular NAD(H) pool. Then, the multienzyme self-assembly system with SpyTag and SpyCatcher effectively channeled intermediates, leading to an 81.1% increase in Allitol titer to 15.03 g/L from 25 g/L d-glucose. This study provided a facilitated strategy for large-scale and efficient biosynthesis of Allitol from a low-cost substrate.