the removal performance of total poly phenols and orthodiphenols (o-diphenols) content in olive mill waste (omw) was investigated with a three stages cross flow laboratory scale rotating biological contactor (rbc) in the present study. due to high cod and other pollutant in the original omw, physico-chemical treatment was effected for cod and other pollutant reduction prior to biological treatm...

The removal performance of total poly phenols and orthodiphenols (o-diphenols) content in olive mill waste (OMW) was investigated with a three stages cross flow laboratory scale rotating biological contactor (RBC) in the present study. Due to high COD and other pollutant in the original OMW, physico-chemical treatment was effected for COD and other pollutant reduction prior to biological tr...

A solvent deuterium isotope effect on the catalytic affinity (km) and catalytic constant (kcat) of tyrosinase in its action on different monophenols and o-diphenols was observed. The catalytic constant decreased in all substrates as the molar fraction of deuterated water in the medium increased, while the catalytic affinity only decreased for the o-diphenols with an R group in C-1 [-H, -CH3 and...

Tyrosinase usually catalyses the conversion of monophenols into o-diphenols and the oxidation of diphenols to the corresponding o-quinones. Sugumaran [(1986) Biochemistry 25, 4489-4492] has previously proposed an unusual oxidative decarboxylation of 3,4-dihydroxymandelate catalysed by tyrosinase. Our determination of the intermediates involved in the reaction demonstrated that 3,4-dihydroxybenz...

Tyrosinase shows kinetic cooperativity in its action on o-diphenols, but not when it acts on monophenols, confirming that the slow step is the hydroxylation of monophenols to o-diphenols. This model can be generalised to a wide range of substrates; for example, type S(A) substrates, which give rise to a stable product as the o-quinone evolves by means of a first or pseudo first order reaction (...

Tyrosinase is a natural enzyme and is often purified to only a low degree and it is involved in a variety of functions which mainly catalyse the o-hydroxylation of monophenols into their corresponding o-diphenols and the oxidation of o-diphenols to o-quinones using molecular oxygen, which then polymerizes to form brown or black pigments. The synthesis of o-diphenols is a potentially valuable ca...

tyrosinase (ec: 1.14.18.1) is a copper - containing enzyme which is distributed in all domains of life such as prokaryote, eukaryote, mammals, invertebrates and plants. tyrosinase catalyzes the oxidation of monophenols to diphenols and diphenols to o-quinones . the tyrosinase crystallographic data shows two histidine -rich regions named cua and cub. a loop containing residues m374, s375 and v37...

The antioxidant activity of the phenolic fraction of extra virgin olive oil was assessed in samples that had a decreasing content of antioxidants in the presence and absence of copper ions as a catalyst of autoxidation. The oxidation process was evaluated by measuring primary and secondary oxidation products. Changes in phenols and tocopherols were investigated by high-performance liquid chroma...

Tetrahydrobiopterine (6BH(4)) can diminish the oxidative stress undergone by keratinocytes and melanocytes by reducing the o-quinones generated by the oxidation of the corresponding o-diphenols. We found that 6BH(4) and their analogs reduced all the o-quinones studied. The formal potentials of different quinone/diphenol pairs indicate that the o-quinones with withdrawing groups are more potent ...