Alkali and halide-resistant catalysis by the multipotent oxidase from Marinomonas mediterranea.
The incorporation of fungal laccases into novel applications has been delayed mainly due to their intrinsic sensitivity towards halides and alkaline conditions. In order to explore new sources of enzymes we evaluated the multipotent polyphenol oxidase PPO1 from the marine bacterium Marinomonas mediterranea. Here we report that, in contrast to its fungal counterparts, PPO1 remained functional above neutral pH presenting high specificity for phenolic compounds, in particular for methoxyl-substituted mono-phenols and catechols. These properties, in addition to its tolerance towards chloride (up to 1 M) and its elevated redox potential at neutral pH (0.9 V), suggest this enzyme may be an interesting candidate for specific applications such as the Amperometric determination of phenolic compounds and bio-fuel cells.
Jimenez-Juarez
Nuria
N
Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, AP 510-3, Cuernavaca, Morelos CP 62250, Mexico.
Roman-Miranda
Rosa
R
Baeza
Alejandro
A
Sánchez-Amat
Antonio
A
Vazquez-Duhalt
Rafael
R
Valderrama
Brenda
B
D002384:Catalysis; D004156:Catechol Oxidase / Q000737:chemistry / Q000378:metabolism*; D002712:Chlorides / Q000494:pharmacology; D020563:Gammaproteobacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D002712:Chlorides; D004156:Catechol Oxidase