EC Number |
Substrates |
Organism |
Products |
Reversibility |
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1.14.13.82 | more |
to detect fungal demethylation and release of catechol-like structures, these are demonstrated using catechol, gallic acid and caffeic acid as standard model compounds to forms mono, bis- and/or tris-catechol-Fe3+ complexes. The catechol-Fe3+ complexes formation controlled by pH via the deprotonation of the catechol hydroxyls is investigated at pH 2.5, 8.0 and 10.0 and demonstrates that catechol formed mono, bis- and/or tris-catechol-Fe3+ complexes, and show maximum absorbance at 547 nm. Lignin demethylation (O-demethylase) and formation of dicatecholic structures is detected. The produced aromatic vicinal diol groups in lignin model compounds (LMCs) and KL are determined using different catecholic-binding reagents with the influence of H2O2, along with 4-antiaminopyrine reagent, and are analyzed by the following: 1. Fe3+-catechol complexation method, 2. HNO2 method, 3. FAS (ferric ammonium-sulfate) method, and 4. Ti(III)-NTA (titanium (III)-nitrilotriacetate) method for hydrolytic zone formation. Among the tested methods, Fe3+-catechol complexation shows lytic zone formation, mechanism, overview |
Aspergillus sp. |
? |
- |
- |
1.14.13.82 | more |
to detect fungal demethylation and release of catechol-like structures, these are demonstrated using catechol, gallic acid and caffeic acid as standard model compounds to forms mono, bis- and/or tris-catechol-Fe3+ complexes. The catechol-Fe3+ complexes formation controlled by pH via the deprotonation of the catechol hydroxyls is investigated at pH 2.5, 8.0 and 10.0 and demonstrates that catechol formed mono, bis- and/or tris-catechol-Fe3+ complexes, and show maximum absorbance at 547 nm. Lignin demethylation (O-demethylase) and formation of pyrocatecholic structures is detected. The produced aromatic vicinal diol groups in lignin model compounds (LMCs) and KL are determined using different catecholic-binding reagents with the influence of H2O2, along with 4-antiaminopyrine reagent, and are analyzed by the following: 1. Fe3+-catechol complexation method, 2. HNO2 method, 3. FAS (ferric ammonium-sulfate) method, and 4. Ti(III)-NTA (titanium (III)-nitrilotriacetate) method for hydrolytic zone formation. Among the tested methods, Fe3+-catechol complexation shows lytic zone formation, mechanism, overview |
Galerina autumnalis |
? |
- |
- |
1.14.13.82 | 3,4,5-trimethoxybenzoate + O2 + NADH + H+ |
70% of the activity compared to vanillate |
Acinetobacter sp. |
3-hydroxy-4,5-dimethoxybenzoate + NAD+ + H2O + formaldehyde |
- |
? |
1.14.13.82 | 3,4,5-trimethoxybenzoate + O2 + NADH + H+ |
70% of the activity compared to vanillate |
Acinetobacter sp. ADP1 |
3-hydroxy-4,5-dimethoxybenzoate + NAD+ + H2O + formaldehyde |
- |
? |
1.14.13.82 | 3,4-dimethoxybenzoate + O2 + NADH + H+ |
- |
Acinetobacter sp. |
isovanillate + NAD+ + H2O + formaldehyde |
- |
? |
1.14.13.82 | 3,4-dimethoxybenzoate + O2 + NADH + H+ |
- |
Acinetobacter sp. ADP1 |
isovanillate + NAD+ + H2O + formaldehyde |
- |
? |
1.14.13.82 | 3-(hydroxymethyl)-benzoate + NAD+ + H2O + formaldehyde |
- |
Acinetobacter sp. |
m-toluate + O2 + NADH + H+ |
- |
? |
1.14.13.82 | 3-(hydroxymethyl)-benzoate + NAD+ + H2O + formaldehyde |
- |
Acinetobacter sp. ADP1 |
m-toluate + O2 + NADH + H+ |
- |
? |
1.14.13.82 | 3-hydroxymethyl-4-hydroxy-5-methylbenzoate + NADH + H+ + ? |
85% of the activity compared to vanillate |
Acinetobacter sp. |
4-hydroxy-3,5-dimethylbenzoate + NAD+ + ? |
- |
? |
1.14.13.82 | 3-hydroxymethyl-4-hydroxy-5-methylbenzoate + NADH + H+ + ? |
85% of the activity compared to vanillate |
Acinetobacter sp. ADP1 |
4-hydroxy-3,5-dimethylbenzoate + NAD+ + ? |
- |
? |