Veratryl alcohol
(Synonyms: 藜芦醇; 3,4-Dimethoxybenzyl alcohol) 目录号 : GC37896
Veratryl alcohol (VA, Veratrole alcohol, 3,4-Dimethoxybenzyl alcohol), a secondary metabolite of some lignin degrading fungi, is the natural substrate of Lignin peroxidase (LiP).
Cas No.:93-03-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Veratryl alcohol (VA, Veratrole alcohol, 3,4-Dimethoxybenzyl alcohol), a secondary metabolite of some lignin degrading fungi, is the natural substrate of Lignin peroxidase (LiP).
[1] Jefferson O Romero, et al. Comput Struct Biotechnol J. 2019 Jul 10;17:1066-1074. [2] M S Leisola, et al. Anal Biochem. 1986 May 15;155(1):108-11.
| Cas No. | 93-03-8 | SDF | |
| 别名 | 藜芦醇; 3,4-Dimethoxybenzyl alcohol | ||
| Canonical SMILES | OCC1=CC=C(OC)C(OC)=C1 | ||
| 分子式 | C9H12O3 | 分子量 | 168.19 |
| 溶解度 | Ethanol: 100 mg/mL (594.57 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 | 5.9457 mL | 29.7283 mL | 59.4566 mL |
| 5 mM | 1.1891 mL | 5.9457 mL | 11.8913 mL |
| 10 mM | 0.5946 mL | 2.9728 mL | 5.9457 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。
Catalytic Oxidation of Veratryl alcohol Derivatives Using RuCo/rGO Composites
Chemistry 2022 Mar 28;28(18):e202104380.PMID:35229376DOI:10.1002/chem.202104380.
Chemoselectively oxidizing Cα -OH to C=O has been considered as a key step for the oxidative depolymerization of lignin. In this work, we design and prepare a series of composites of RuCo alloy nanoparticles and reduced graphene oxide (RuCo/rGO) with different Ru to Co ratios and explore their catalytic activities in the oxidation of Veratryl alcohol derivatives, which usually serve as the model compounds for studying lignin oxidation. It is illustrated that the Ru to Co ratio determines the morphology and average size of the RuCo alloy nanoparticles on rGO, and the overall catalytic activities of the composites. The RuCo alloy nanoparticles on rGO with Ru to Co ratios of 1 : 0 to 1.2 : 1 show a unique flower-shaped morphology that increases the exposure of the active sites and thus promotes their contact with the substrates. The RuCo/rGO composites exhibit high catalytic activities for the oxidation of Cα -OH to aldehydes at 100 °C for 2 h. Additionally, the Co component affords the RuCo/rGO composites with magnetic properties that make the separation and recovery of the catalyst simple. Given the high catalytic performances and easy recovery, the RuCo/rGO composites would be potentially useful for the depolymerization of lignin.
Sugar oxidoreductases and Veratryl alcohol oxidase as related to lignin degradation
J Biotechnol 1997 Mar 14;53(2-3):115-31.PMID:9177041DOI:10.1016/s0168-1656(97)01680-5.
Properties of cellobiose:quinone oxidoreductase (CBQ), cellobiose dehydrogenase (CDH), glyoxal oxidase (GLOX), glucose oxidases and Veratryl alcohol oxidase (VAO) are reviewed. There is strong evidence that CDH reduces quinones, phenoxy and cation radicals. Glucose oxidases (glucose 1-oxidase and pyranose 2-oxidase) and VAO have been less investigated but evidence for reduction of the above compounds is accumulating. Pyranose oxidase, glyoxal oxidase and VAO are very important for hydrogen peroxide production by white-rot fungi. CDH is only produced on cellulose or on wood, whereas pyranose oxidase and VAO are produced both on wood and on rich glucose media suggesting that the lignin degrading white-rot fungi may use different quinone and radical reducing enzymes to regulate lignin polymerization/depolymerization depending on the substrate and cultivation conditions. Intracellular quinone reductases are also produced. Whether brown-rot fungi in general produce CBQ/CDH or VAO is not clear. The Fe(III) reducing ability of both CDH and certain phenolate compounds agree with the rapid depolymerization of cellulose by brown-rot fungi. The interaction of Fe(III) reduction with the hydrogen peroxide producing system in white-rot and brown-rot fungi requires more investigation.
Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju
Biochem J 1988 Oct 15;255(2):445-50.PMID:3060110DOI:10.1042/bj2550445.
The basidiomycete Pleurotus sajor-caju mineralizes ring-14C-labelled lignin (dehydrogenative polymer) when grown in mycological broth. Under these conditions, two Veratryl alcohol oxidase (VAO) enzymes were found in the culture medium. They oxidized a number of aromatic alcohols to aldehydes and reduced O2 to H2O2. The enzymes were purified by ion-exchange and gel-permeation chromatography. The final step of purification on Mono Q resolved the activity into two peaks (VAO I and VAO II). Both enzymes had the same Mr, approx. 71,000, but their isoelectric points differed slightly, 3.8 for VAO I and 4.0 for VAO II. Their amino acid compositions were similar except for aspartic acid/asparagine and glycine. Both enzymes are glycoproteins and contain flavin prosthetic groups. Their pH optima were around 5, and kinetic constants and specificities were similar. 4-Methoxybenzyl alcohol was oxidized the most rapidly, followed by Veratryl alcohol. Not all aromatic alcohols were oxidized, neither were non-aromatic alcohols. Cinnamyl alcohol was oxidized at the gamma position. The VAO enzymes thus represent a significantly different route for Veratryl alcohol oxidation from that catalysed by the previously found lignin peroxidases from Phanerochaete chrysosporium. The role of the oxidases in biodegradation might be to produce H2O2 during oxidation of lignin fragments.
Structure of dye-decolorizing peroxidase from Bacillus subtilis in complex with Veratryl alcohol
Int J Biol Macromol 2021 Dec 15;193(Pt A):601-608.PMID:34687768DOI:10.1016/j.ijbiomac.2021.10.100.
Dye-decolorizing peroxidases (DyPs) are heme-containing peroxidases, which have promising application in biodegradation of phenolic lignin compounds and in detoxification of dyes. In this study, the crystal structure of BsDyP- Veratryl alcohol (VA) complex delves deep into the binding of small substrate molecules within the DyP heme cavity. The biochemical analysis shows that BsDyP oxidizes the VA with a turnover number of 0.065 s-1, followed by the oxidation of 2,6-dimethoxyphenol (DMP) and guaiacol with a comparable turnover number (kcat) of 0.07 s-1 and 0.07 s-1, respectively. Moreover, biophysical and computational studies reveal the comparable binding affinity of substrates to BsDyP and produce lower-energy stable BsDyP-ligand(s) complexes. All together with our previous findings, we are providing a complete structural description of substrate-binding sites in DyP. The structural insight of BsDyP helps to modulate its engineering to enhance the activity towards the oxidation of a wide range of substrates.
Veratryl alcohol stimulates fruiting body formation in the oyster mushroom, Pleurotus ostreatus
FEMS Microbiol Lett 2001 Jan 15;194(2):235-8.PMID:11164314DOI:10.1111/j.1574-6968.2001.tb09475.x.
The oyster mushroom, Pleurotus ostreatus, cultivated in solid state on sugarcane bagasse-wheat bran (5:1) medium in the presence of Veratryl alcohol resulted in an increased production of the fruiting body at earlier times compared to when the fungus was grown in the absence of Veratryl alcohol. The results indicate a new physiological role for Veratryl alcohol in stimulating fruiting body formation. Veratryl alcohol also stimulated laccase production during the mycelial growth stage. Evidence is also presented that laccases were involved in the physiological development of the fruiting body.