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• W2038851230 abstract "The reduction of dioxygen by cellobiose oxidase leads to accumulation of H 2 O 2 , with either cellobiose or microcrystalline cellulose as electron donor. Cellobiose oxidase will also reduce many Fe(III) complexes, including Fe(III) acetate. Many Fe(II) complexes react with H 2 O 2 to produce hydroxyl radicals or a similarly reactive species in the Fenton reaction as shown: H 2 O 2 + Fe 2+ → HO • + HO − + Fe 3+ . The hydroxylation of salicylic acid to 2,3‐dihydroxybenzoic acid and 2,5‐dihydroxybenzoic acid is a standard test for hydroxyl radicals. Hydroxylation was observed in acetate buffer (pH 4.0), both with Fe(II) plus H 2 O 2 and with cellobiose oxidase plus cellobiose, O 2 and Fe(III). The hydroxylation was suppressed by addition of catalase or the absence of iron [Fe(II) or Fe(III) as appropriate]. Another test for hydroxyl radicals is the conversion of deoxyribose to malondialdehyde; this gave positive results under similar conditions. Further experiments used an O 2 electrode. Addition of H 2 O 2 to Fe(II) acetate (pH 4.0) or Fe(II) phosphate (pH 2.8) in the absence of enzyme led to a pulse of O 2 uptake, as expected from production of hydroxyl radicals as shown: RH + HO • → R • + H 2 O;R • + O 2 → RO • 2 → products. With phosphate (pH 2.8) or 10 mM acetate (pH 4.0), the O 2 uptake pulse was increased by Avicel, suggesting that the Avicel was being damaged. Oxygen uptake was monitored for mixtures of Avicel (5 g · 1 −1 ), cellobiose oxidase, O 2 and Fe(III) (30 μM). An addition of catalase after 20–30 min indicated very little accumulation of H 2 O 2 , but caused a 70% inhibition of the O 2 uptake rate. This was observed with either phosphate (pH 2.8) or 10 mM acetate (pH 4.0) as buffer, and is further evidence that oxidative damage had been taking place, until the Fenton reaction was suppressed by catalase. A separate binding study established that with 10 mM acetate as buffer, almost all (98%) of the Fe(III) would have been bound to the Avicel. In the presence of Fe(III), cellobiose oxidase could provide a biological method for disrupting the crystalline structure of cellulose." @default.
• W2038851230 created "2016-06-24" @default.
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• W2038851230 date "1992-09-01" @default.
• W2038851230 modified "2023-10-15" @default.
• W2038851230 title "Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of <i>Phanerochaete chrysosporium</i>" @default.
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• W2038851230 doi "https://doi.org/10.1111/j.1432-1033.1992.tb17251.x" @default.
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