Sophorose
(Synonyms: Α-2-葡糖-Β-葡糖苷) 目录号 : GC41090
A disaccharide component of sophorolipids
Cas No.:20429-79-2
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
Sophorose is a disaccharide component of the microbial glycolipids produced by yeast termed sophorolipids. Due to their hydrophobic nature, sophorolipids are often employed as biosurfactants. Sophorolipids also demonstrate antibacterial, antifungal, spermicidal, virucidal, and anti-cancer activities. Sophorose has been identified as a potent inducer of cellulase gene expression in studies of T. reesei fermentation.
| Cas No. | 20429-79-2 | SDF | |
| 别名 | Α-2-葡糖-Β-葡糖苷 | ||
| Canonical SMILES | O[C@@H]1[C@@H](O[C@@]2([H])[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O2)C(O)O[C@H](CO)[C@H]1O | ||
| 分子式 | C12H22O11 | 分子量 | 342.3 |
| 溶解度 | Water: soluble | 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 | 2.9214 mL | 14.6071 mL | 29.2141 mL |
| 5 mM | 0.5843 mL | 2.9214 mL | 5.8428 mL |
| 10 mM | 0.2921 mL | 1.4607 mL | 2.9214 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。
Sophorose metabolism and cellulase induction in Trichoderma
Arch Microbiol 1977 May 13;113(1-2):61-4.PMID:560832DOI:10.1007/BF00428581.
The cellulase inducer Sophorose was rapidly catabolized to CO2 and H2O by Trichoderma: only small amounts were used to induce the synthesis of cellulase. 3H-sophorose uptake began after a lag of 1 h and its half-life in the medium was less than 5 h. Cellulase activity in the medium did not increase till 6 h after the addition of Sophorose and reached a half maximum value at 14 h. The presence of free Sophorose in the medium was required for continuous cellulase production. Several small Sophorose addition induced much more cellulase than an equivalent single dose. These results are attributed to two pathways of Sophorose utilization, a catabolic pathway that has a high capacity but low affinity for Sophorose and an inductive pathway having a lower capacity but higher affinity for Sophorose.
Sophorose as an inducer of cellulase in Trichoderma viride
J Bacteriol 1962 Feb;83(2):400-8.PMID:14469205DOI:10.1128/jb.83.2.400-408.1962.
Mandels, Mary (Quartermaster Research and Engineering Center, Natick, Mass.), Fredrick W. Parrish, and Elwyn T. Reese. Sophorose as an inducer of cellulase in Trichoderma viride. J. Bacteriol. 83:400-408. 1962.-The impurity in glucose responsible for cellulase induction in Trichoderma viride QM 6a has been isolated and characterized as Sophorose (2-O-beta-d-glucopyranosyl-d-glucose). It is present at 0.0058% in reagent grade glucose. Sophorose is a very powerful inducer of cellulase for Trichoderma viride, being 2500 times as active as cellobiose. Modifications of Sophorose, such as reduction or glycoside formation, destroy its inducing ability. The high activity of Sophorose as an inducer is specific for T. viride.
Epimerization and Decomposition of Kojibiose and Sophorose by Heat Treatment under Neutral pH Conditions
J Appl Glycosci (1999) 2019 Jan 20;66(1):1-9.PMID:34354514DOI:10.5458/jag.jag.JAG-2018_0002.
We evaluated the stabilities of kojibiose and Sophorose when heated under neutral pH conditions. Kojibiose and Sophorose epimerized at the C-2 position of glucose on the reducing end, resulting in the production of 2-O-α-D-glucopyranosyl-D-mannose and 2-O-β-D-glucopyranosyl-D-mannose, respectively. Under weak alkaline conditions, kojibiose was decomposed due to heating into its mono-dehydrated derivatives, including 3-deoxy-2,3-unsaturated compounds and bicyclic 3,6-anhydro compounds. Following these experiments, we propose a kinetic model for the epimerization and decomposition of kojibiose and Sophorose by heat treatment under neutral pH and alkaline conditions. The proposed model shows a good fit with the experimental data collected in this study. The rate constants of a reversible epimerization of kojibiose at pH 7.5 and 90 °C were (1.6 ± 0.1) × 10-5 s-1 and (3.2 ± 0.2) × 10-5 s-1 for the forward and reverse reactions, respectively, and were almost identical to those [(1.5 ± 0.1) × 10-5 s-1 and (3.5 ± 0.4) × 10-5 s-1] of Sophorose. The rate constant of the decomposition reaction for kojibiose was (4.7 ± 1.1) × 10-7 s-1 whereas that for Sophorose [(3.7 ± 0.2) × 10-6 s-1] was about ten times higher. The epimerization reaction was not significantly affected by the variation in the buffer except for a borate buffer, and depended instead upon the pH value (concentration of hydroxide ions), indicating that epimerization occurred as a function of the hydroxide ion. These instabilities are an extension of the neutral pH conditions for keto-enol tautomerization that are often observed under strong alkaline conditions.
Comparative metabolism of cellulose, Sophorose and glucose in Trichoderma reesei using high-throughput genomic and proteomic analyses
Biotechnol Biofuels 2014 Mar 21;7(1):41.PMID:24655731DOI:10.1186/1754-6834-7-41.
Background: The filamentous fungus Trichoderma reesei is a major producer of lignocellulolytic enzymes utilized by bioethanol industries. However, to achieve low cost second generation bioethanol production on an industrial scale an efficient mix of hydrolytic enzymes is required for the deconstruction of plant biomass. In this study, we investigated the molecular basis for lignocellulose-degrading enzyme production T. reesei during growth in cellulose, Sophorose, and glucose. Results: We examined and compared the transcriptome and differential secretome (2D-DIGE) of T. reesei grown in cellulose, Sophorose, or glucose as the sole carbon sources. By applying a stringent cut-off threshold 2,060 genes were identified as being differentially expressed in at least one of the respective carbon source comparisons. Hierarchical clustering of the differentially expressed genes identified three possible regulons, representing 123 genes controlled by cellulose, 154 genes controlled by Sophorose and 402 genes controlled by glucose. Gene regulatory network analyses of the 692 genes differentially expressed between cellulose and Sophorose, identified only 75 and 107 genes as being specific to growth in Sophorose and cellulose, respectively. 2D-DIGE analyses identified 30 proteins exclusive to Sophorose and 37 exclusive to cellulose. A correlation of 70.17% was obtained between transcription and secreted protein profiles. Conclusions: Our data revealed new players in cellulose degradation such as accessory proteins with non-catalytic functions secreted in different carbon sources, transporters, transcription factors, and CAZymes, that specifically respond in response to either cellulose or Sophorose.
New-to-nature Sophorose analog: a potent inducer for gene expression in Trichoderma reesei
Enzyme Microb Technol 2016 Apr;85:44-50.PMID:26920480DOI:10.1016/j.enzmictec.2016.01.003.
Controlled hydrolysis of lactonic sophorolipids from Starmerella bombicola yields a previously undescribed Sophorose analog that potently induces cellulase in Trichoderma reesei Rut-C30. Acid treatment of natural sophorolipids results in a mixture of monoacetylated, deacetylated, and diacetylated sophorolipids in acidic and lactonic forms. Isolation of the active components of the mixture, followed by structure determination by MS and NMR, reveals a new chemical entity, in which the lactone ring has been opened at the C-1' rather than at the C-4″ position of the Sophorose moiety. This Sophorose ester is resistant to degradation by the host and is at least 28 times more powerful an inducer than Sophorose in shake-flask culture. Even at low concentrations (0.05 mM), the chemically modified sophorolipid effectively induces cellulase. With further improvements, this highly enabling technology can potentially reduce the cost of enzymes produced in T. reesei and can facilitate the rapid deployment of enzyme plants to support the nascent cellulosic biofuels and biochemicals industries.