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The key role of catechol oxidase in enzymatic browning makes it a common target for inhibition. While a number of inhibitory strategies exist such as high temperature treatments(70-90 °C) to eliminate catechol oxidase catalytic activity, [6] a popular strategy is decreasing the pH with citric acid. Catechol oxidase is more catalytically active ...
Thus, the two substrates of this enzyme are catechol and O 2, whereas its two products are [[dibenzo[1,4]dioxin-2,3-dione]] and H 2 O. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is catechol:oxygen oxidoreductase ...
Catechol (/ ˈ k æ t ɪ tʃ ɒ l / or / ˈ k æ t ɪ k ɒ l /), also known as pyrocatechol or 1,2-dihydroxybenzene, is an organic compound with the molecular formula C 6 H 4 (OH) 2. It is the ortho isomer of the three isomeric benzenediols .
When the surface of apples are exposed to the oxygen in the air, the oxidative enzymes like polyphenol oxidase and catechol oxidase oxidize the fruit (electrons are lost to the air). Such browning can be prevented by cooking the fruit or lowering the pH (which destroys, inactivates, or denatures the enzyme) or by preventing oxygen from getting ...
Thus, the two substrates of this enzyme are cis-1,2-dihydrobenzene-1,2-diol and NAD +, whereas its 3 products are catechol, NADH, and H +. This enzyme belongs to the family of oxidoreductases , specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor.
Figure 1. The overall reaction of catechol 1,2-dioxygenase. Using a non-heme iron(III) complex, 1,2-CTD is able to oxidatively cleave catechol into cis,cis-muconic acid. More specifically, 1,2-CTD is an intradiol dioxygenase, a family of catechol dioxygenases that cleaves the bond between the phenolic hydroxyl groups of catechol using an Fe 3 ...
The tricopper site found in many laccases; note that each copper center is bound to the imidazole sidechains of histidines (color code: copper is brown, nitrogen is blue).. The active site consists of four copper centers, which adopt structures classified as type I, type II, and type III.
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