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Oxidative enzymes such as phenol oxidase and peroxidase mediate lignin degradation and humification. [47] Phenol oxidase activity is quantified by oxidation of L-3, 4-dihydoxyphenylalanine (L-DOPA), pyrogallol (1, 2, 3-trihydroxybenzene), or ABTS (2, 2’-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid).
Although laccase is known to crosslink AX, under the microscope it was found that the laccase also acted on the flour proteins. Oxidation of the ferulic acid on AX to form ferulic acid radicals increased the oxidation rate of free SH groups on the gluten proteins and thus influenced the formation of S-S bonds between gluten polymers. [13]
Laccase EC 1.10.3.2 (urishiol oxidase), a 3-domain enzyme found in fungi and plants, which oxidizes different phenols and diamines. CueO is a laccase found in Escherichia coli that is involved in copper-resistance. [4] Ascorbate oxidase EC 1.10.3.3, a 3-domain enzyme found in higher plants.
The Chaetomiaceae are a family of fungi in the Ascomycota, order Sordariales, [1] class Sordariomycetes. [2] Chaetomiaceae are usually saprobic or parasitic. [1] Cheatomiaceae are a great source of enzymes with diverse biotechnological and industrial applications such as PMO (polysaccharide monooxygenase), L-methioninase, β-1,3-glucanase, laccase, dextranase, lipolytic, pectinolytic ...
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Water is released, and the second o-quinone product is formed together with the restoration of the initial Cu(II)-Cu(II) state to complete the catalytic cycle. [ 15 ] This proposed catalytic cycle is supported by the experimental observation that stoichiometric amounts of o-quinone form after catechol addition to the enzyme, even when dioxygen ...
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The enzyme works by catalyzing the o-hydroxylation of monophenol molecules in which the benzene ring contains a single hydroxyl substituent to o-diphenols (phenol molecules containing two hydroxyl substituents at the 1, 2 positions, with no carbon between). [3] It can also further catalyse the oxidation of o-diphenols to produce o-quinones. [4]
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