Search results for "Ascorbate oxidase"

showing 3 items of 3 documents

Laccases: structure, reactions, distribution

2004

Laccases (EC 1.10.3.2, p-diphenol: dioxygen oxidoreductases) are multi-copper proteins that use molecular oxygen to oxidize various aromatic and non-aromatic compounds by a radical-catalyzed reaction mechanism. The enzymes are involved in the pathogenicity, immunity and morphogenesis of organisms and in the metabolic turnover of complex organic substances such as lignin or humic matter. Owing to their high non-specific oxidation capacity, laccases are useful biocatalysts for diverse biotechnological applications. Until recently, laccases were only found in eukaryotes (fungi, higher plants, insects), but now there is strong evidence for their widespread distribution in prokaryotes and the fi…

chemistry.chemical_classificationLaccaseProtein familyLaccaseGeneral Physics and AstronomyAscorbate OxidaseCell BiologyBiologyPathogenicityCatalysischemistry.chemical_compoundEnzymeBiochemistrychemistryStructural BiologyAnimalsLigninGeneral Materials ScienceMolecular oxygenBilirubin oxidaseCopperMicron
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Interaction of sodium, lithium, caesium, and potassium ions with ascorbyl radicals.

1987

Abstract The influence of the concentration of sodium, lithium , caesium, and potassium ions as well as of the ionic strength of the solutions used on the dismutation rate of ascorbyl radicals has been investigated. While the dismutation rate was not influenced by Li+, it decreased, however, with increasing concentrations of the other ions investigated. The largest effect was obtained with Na+. This change in dismutation rate indicates a stabilizing effect on ascorbyl radical by these ions.

Free RadicalsSodiumRadicalInorganic chemistryOsmolar ConcentrationSodiumchemistry.chemical_elementCesiumAscorbic AcidLithiumPotassium ionsAscorbic acidGeneral Biochemistry Genetics and Molecular BiologyIonchemistryIonic strengthCaesiumPotassiumAscorbate OxidaseLithiumZeitschrift fur Naturforschung. C, Journal of biosciences
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DEGRADATIVE ENZYMATIC ACTIVITIES IN FRESH-CUT BLOOD ORANGE SLICES DURING CHILLED STORED

2009

Summary Blood-orange fruits are suitable to fresh-cut fruit production because of their chemical compositions. Nevertheless, the main limitation of using freshly cut oranges is their susceptibility to juiciness loss and ascorbic acid degradation because of enzymatic alterations. The aim of this work is: to identify some of the enzymes causing the qualitative decay in blood-orange slices during 15 days of chilled storage (at 4 ± 0.5 °C and 85% RH); to investigate the susceptibility to the previous alterations of five blood-orange clones (Moro nucellare, Sanguinello nucellare, Tarocco arcimusa, Tarocco gallo and Tarocco meli) to select the most suitable one for fresh-cut production. The enzym…

biologyChemistryFood preservationCold storageOrange (colour)Ascorbate oxidase pectinmethylesterase polyphenol oxidase quality control.Ascorbic acidPolyphenol oxidaseIndustrial and Manufacturing EngineeringEnzyme assayBiochemistrybiology.proteinBrowningFood scienceCatechol oxidaseFood Science
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