Coupled Oxidation of Coniferyl Alcohol by Peroxidase-yellow Enzyme System
نویسندگان
چکیده
منابع مشابه
Spectroscopic analyses of the biofuels-critical phytochemical coniferyl alcohol and its enzyme-catalyzed oxidation products.
Lignin composition (monolignol types of coniferyl, sinapyl or p-coumaryl alcohol) is causally related to biomass recalcitrance. We describe multiwavelength (220, 228, 240, 250, 260, 290, 295, 300, 310 or 320 nm) absorption spectroscopy of coniferyl alcohol and its laccase- or peroxidase-catalyzed products during real time kinetic, pseudokinetic and endpoint analyses, in optical turn on or turn ...
متن کاملHitherto unrecognized fluorescence properties of coniferyl alcohol.
We instituted a quasi-quality assurance program for demonstrating coniferyl alcohol's fluorescence and fluorescence diminishment following enzymatic oxidation. The magnitude of diminishment was a measure of catalysis. High throughput screening was performed in pseudo-kinetic and endpoint modes by measuring the fluorescence at 416 nm following excitation at 290, 310 or 340 nm. Dose-response trac...
متن کاملAnaerobic degradation of coniferyl alcohol by methanogenic consortia.
[This corrects the article on p. 1445 in vol. 46.].
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Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both ...
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ژورنال
عنوان ژورنال: The Journal of the Society of Chemical Industry, Japan
سال: 1958
ISSN: 0023-2734,2185-0860
DOI: 10.1246/nikkashi1898.61.1068