Application | Comment | Organism |
---|---|---|
synthesis | enzymatic oxidative polymerization of dihydroquercetin from Larix sibirica using bilirubin oxidase as a biocatalyst. As compared with the monomer, oligoDHQ demonstrates higher thermal stability and high antioxidant activity | Albifimbria verrucaria |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Albifimbria verrucaria |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Albifimbria verrucaria | Q12737 | - |
- |
Purification (Comment) | Organism |
---|---|
the commercial preparation of bilirubin oxidase from Myrothecium verrucaria is additionally purified by anion exchange chromatography | Albifimbria verrucaria |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Albifimbria verrucaria | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2 | - |
Albifimbria verrucaria | ? + H2O | - |
? | |
ferricyanide + O2 | - |
Albifimbria verrucaria | ? + H2O | - |
? | |
additional information | oxidative polymerization of dihydroquercetin from Larix sibirica using bilirubin oxidase as a biocatalyst. DHQ oligomers (oligoDHQ) with molecular mass of 2800 and polydispersity of 8.6 are obtained by enzymatic reaction under optimal conditions. The oligomers appear to be soluble in dimethylsulfoxide, dimethylformamide, and methanol. UVvisible spectra of oligoDHQ in dimethylsulfoxide indicate the presence of highly conjugated bonds. Irregular structure of a polymer formed via the enzymatic oxidation of DHQ followed by nonselective radical polymerization. As compared with the monomer, oligoDHQ demonstrates higher thermal stability and high antioxidant activity | Albifimbria verrucaria | ? | - |
? |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 9.5 | activity range, inactive above and below. In reaction with electron donor substrates, the enzyme exhibits the maximal activity at acidic pH values: pH 4.0 for 2,2'-azino-bis-[3-ethylbenzthiazoline-6-sulfonic acid] (ABTS) and pH 3.0 for potassium ferricyanide. Catalytic activity decreases on pH increase, and the enzyme becomes completely inactive at pH above 9.5. At neutral pH values, bilirubin oxidase retains about 50% maximal activity in oxidation of both substrates. In reaction with a hydrogen atom donor (catechol), the pH profile of the enzyme activity is shifted to alkaline values: enzymatic activity is not exhibited at pH below 6.0. This is probably related with the higher reactivity of the substrate as a phenolate anion | Albifimbria verrucaria |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is a copper-containing oxidase that catalyzes oxidation of various organic compounds, including phenolic ones, by molecular oxygen, the latter is reduced to water via a fourelectron mechanism | Albifimbria verrucaria |