This product is isolated and purified from the roots of Beta vulgaris
(3,4-Dimethoxyphenyl)methanol/3,4-Diamethoxybenzyl Methanol/3,4-Dimethoxybenzyl Alcohol/3,4-DIMETHOXYPHENYLMETHYL ALCOHOL/Benzenemethanol, 3,4-dimethoxy-/Veratrole alcohol/Veratryl alcohol (8CI)/Veratryl Alcohol/benzyl alcohol, 3,4-dimethoxy-
FEBS Lett. 1987 Sep 14;221(2):327-31. Regiospecific oxygenations during ring cleavage of a secondary metabolite, 3,4-dimethoxybenzyl alcohol catalyzed by lignin peroxidase.[Pubmed: 3622773]METHODS AND RESULTS:Enzymatic oxidation of veratryl alcohol yielded a new ring cleavage product (delta-lactone) in addition to the two known gamma-lactone products. The experiment with 18O-enriched water and dioxygen clearly showed that one oxygen atom each from water and dioxygen is specifically incorporated into the cleavage product at the original C3 or C4 position of 3,4-Dimethoxybenzyl Alcohol. CONCLUSIONS:A new type of reaction mechanism proposed for the ring cleavage of this compound is rationally explained in good accord with the one-electron transfer mechanism.
298.1±0.0 °C at 760 mmHg
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provides coniferyl ferulate(CAS#:93-03-8) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. However, low-molecular-weight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases (LPs, EC 126.96.36.199) fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol (VA) to its aryl cation radical (VA+•), releasing it to act as a one-electron lignin oxidant within woody plant cell walls. Here, we attached the fluorescent oxidant sensor BODIPY 581/591 throughout beads with a nominal porosity of 6 kDa and assessed whether peroxidase-generated aryl cation radical systems could oxidize the beads. As positive control, we used the 1,2,4,5-tetramethoxybenzene (TMB) cation radical, generated from TMB by horseradish peroxidase. This control oxidized the beads to depths that increased with the amount of oxidant supplied, ultimately resulting in completely oxidized beads. A reaction-diffusion computer model yielded oxidation profiles that were within the 95% confidence intervals for the data. By contrast, bead oxidation caused by VA and the LPA isozyme of Phanerochaete chrysosporium was confined to a shallow shell of LP-accessible volume at the bead surface, regardless of how much oxidant was supplied. This finding contrasted with the modeling results, which showed that if the LP/VA system were to release VA+•, it would oxidize the bead interiors. We conclude that LPA releases insignificant quantities of VA+• and that a different mechanism produces small ligninolytic oxidants during white rot.
Phanerochaete chrysosporium; biodegradation; computer modeling; confocal microscopy; free radicals; imaging; lignin degradation; peroxidase; white rot fungus
Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant.
Houtman CJ1, Maligaspe E1, Hunt CG1, Fernandez-Fueyo E2, Martinez AT2, Hammel KE3,4.
2018 Mar 30
Multiplicity in laccases among lignin degrading fungal species is of interest as it confers the ability to degrade several types of lignocellulosics. The combination of laccases produced on such substrates could be beneficial for treatment of complex aromatics, including dyes. In this study, we report on production of high units (679.6Ug-1 substrate) of laccase on solid wheat bran (WB) by Cyathus bulleri. Laccase, purified from the culture filtrates of WB grown fungus, was effective for oxidation of veratryl alcohol, Reactive blue 21 and textile effluent without assistance of externally added mediators. De novo sequencing of the ‘purified’ laccase lead to identification of several peptides that originated from different laccase genes. Transcriptome analysis of the fungus, cultivated on WB, confirmed presence of 8 isozymes, that were re-amplified and sequenced from the cDNA prepared from WB grown fungus. The 8 isozymes were grouped into 3 classes, based on their sequence relationship with other basidiomycete laccases. The isoforms produced on WB decolorized (by ∼57%) and degraded textile effluent far more effectively, compared to laccase obtained from Basal salt cultivated fungus. The decolorization and degradation was also accompanied by more than 95% reduction in phytotoxicity.
Copyright © 2017 Elsevier B.V. All rights reserved.
Cyathus bulleri; Denim effluent; Direct scarlet B degradation; Laccase isoforms; Lignocellulosic wastes
Identification and evaluation of bioremediation potential of laccase isoforms produced by Cyathus bulleri on wheat bran.
Vats A1, Mishra S2.
2018 Feb 15
Pseudomonas putida CSV86 degrades lignin-derived metabolic intermediates, viz, veratryl alcohol, ferulic acid, vanillin, and vanillic acid, as the sole sources of carbon and energy. Strain CSV86 also degraded lignin sulfonate. Cell respiration, enzyme activity, biotransformation, and high-pressure liquid chromatography (HPLC) analyses suggest that veratryl alcohol and ferulic acid are metabolized to vanillic acid by two distinct carbon source-dependent inducible pathways. Vanillic acid was further metabolized to protocatechuic acid and entered the central carbon pathway via the β-ketoadipate route after ortho ring cleavage. Genes encoding putative enzymes involved in the degradation were found to be present at fer, ver, and van loci. The transcriptional analysis suggests a carbon source-dependent cotranscription of these loci, substantiating the metabolic studies. Biochemical and quantitative real-time (qRT)-PCR studies revealed the presence of two distinct O-demethylases, viz, VerAB and VanAB, involved in the oxidative demethylation of veratric acid and vanillic acid, respectively. This report describes the various steps involved in metabolizing lignin-derived aromatic compounds at the biochemical level and identifies the genes involved in degrading veratric acid and the arrangement of phenylpropanoid metabolic genes as three distinct inducible transcription units/operons. This study provides insight into the bacterial degradation of lignin-derived aromatics and the potential of P. putida CSV86 as a suitable candidate for producing valuable products.IMPORTANCEPseudomonas putida CSV86 metabolizes lignin and its metabolic intermediates as a carbon source. Strain CSV86 displays a unique property of preferential utilization of aromatics, including for phenylpropanoids over glucose. This report unravels veratryl alcohol metabolism and genes encoding veratric acid O-demethylase, hitherto unknown in pseudomonads, thereby providing new insight into the metabolic pathway and gene pool for lignin degradation in bacteria. The biochemical and genetic characterization of phenylpropanoid metabolism makes it a prospective system for its application in producing valuable products, such as vanillin and vanillic acid, from lignocellulose. This study supports the immense potential of P. putida CSV86 as a suitable candidate for bioremediation and biorefinery.
Copyright © 2017 American Society for Microbiology.
O-demethylase; Pseudomonas; enzyme induction; phenylpropanoid metabolism; transcription analysis; veratryl alcohol degradation
Carbon Source-Dependent Inducible Metabolism of Veratryl Alcohol and Ferulic Acid in Pseudomonas putida CSV86.
Mohan K1, Phale PS2.
2017 Mar 31