Syringol
Syringol structure
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Common Name | Syringol | ||
|---|---|---|---|---|
| CAS Number | 91-10-1 | Molecular Weight | 154.163 | |
| Density | 1.1±0.1 g/cm3 | Boiling Point | 264.5±0.0 °C at 760 mmHg | |
| Molecular Formula | C8H10O3 | Melting Point | 50-57 °C(lit.) | |
| MSDS | Chinese USA | Flash Point | 99.9±21.8 °C | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Lignin Modification for Biopolymer/Conjugated Polymer Hybrids as Renewable Energy Storage Materials.
ChemSusChem 8 , 4081-5, (2015) Lignin derivatives, which arise as waste products from the pulp and paper industry and are mainly used for heating, can be used as charge storage materials. The charge storage function is a result of the quinone groups formed in the lignin derivative. Herein,... |
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Cellular apoptosis and cytotoxicity of phenolic compounds: a quantitative structure-activity relationship study.
J. Med. Chem. 48 , 7234-42, (2005) In this comprehensive study on the caspase-mediated apoptosis-inducing effect of 51 substituted phenols in a murine leukemia cell line (L1210), we determined the concentrations needed to induce caspase activity by 50% (I50) and utilized these data to develop ... |
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Malachite green decolorization by the filamentous fungus Myrothecium roridum--Mechanistic study and process optimization.
Bioresour. Technol. 194 , 43-8, (2015) The filamentous fungus Myrothecium roridum isolated from a dye-contaminated area was investigated in terms of its use for the treatment of Malachite green (MG). The mechanisms involved in this process were established. Peroxidases and cytochrome P-450 do not ... |
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Versatile peroxidase of Bjerkandera fumosa: substrate and inhibitor specificity.
Enzyme Microb. Technol. 52(1) , 44-53, (2013) The inhibitor and substrate specificities of versatile peroxidase from Bjerkandera fumosa (VPBF) were studied. Two different effects were found: NaN(3), Tween-80, anthracene, and fluorene decreased the activity of VPBF, but p-aminobenzoic acid increased it. A... |
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Laccase-like enzyme activities from chlorophycean green algae with potential for bioconversion of phenolic pollutants.
FEMS Microbiol. Lett. 362 , (2015) In order to explore the abundance and potential environmental functions of green algal laccases, we screened various algae for extracellular laccase-like activities, characterized basic features of these activities in selected species and exemplarily studied ... |
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Crystal structures of dye-decolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol.
FEBS Lett. 586(24) , 4351-6, (2012) The structure of dye-decolorizing peroxidase (DyP)-type peroxidase differs from that of other peroxidase families, indicating that DyP-type peroxidases have a different reaction mechanism. We have determined the crystal structures of DyP with ascorbic acid an... |
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Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.
Biochem. J. 466(2) , 253-62, (2015) Dye-decolorizing peroxidase (DyP) of Auricularia auricula-judae has been expressed in Escherichia coli as a representative of a new DyP family, and subjected to mutagenic, spectroscopic, crystallographic and computational studies. The crystal structure of DyP... |
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Fostering the action of versatile peroxidase as a highly efficient biocatalyst for the removal of endocrine disrupting compounds.
New Biotechnology 33 , 187-95, (2015) Response surface methodology (RSM) was used to optimize the removal of five endocrine disrupting compounds (EDCs) by the enzyme versatile peroxidase (VP): bisphenol A (BPA), triclosan (TCS), estrone (E1), 17β-estradiol (E2) and 17α-ethinylestradiol (EE2). The... |
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Efficient secretory production of CotA-laccase and its application in the decolorization and detoxification of industrial textile wastewater.
Environ. Sci. Pollut. Res. Int. 22 , 9515-23, (2015) Fungal laccases are typically unstable at high pH and temperature conditions, which limit their application in the decolorization of textile wastewater. By contrast, the highly stable bacterial laccases can function within a wider pH range and at high tempera... |
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Continuous removal of endocrine disruptors by versatile peroxidase using a two-stage system.
Biotechnol. Prog. 31 , 908-16, (2015) The oxidant Mn(3+) -malonate, generated by the ligninolytic enzyme versatile peroxidase in a two-stage system, was used for the continuous removal of endocrine disrupting compounds (EDCs) from synthetic and real wastewaters. One plasticizer (bisphenol-A), one... |