One Health collaboration with and among EU Agencies - Bridging research and policy.

In the coming decade, Europe will dedicate billions of euros to the necessary research and innovation (R&I) to support a transition to safe and sustainable food systems. EU Agencies, individually and even more so collectively, can make a difference in supporting the European research agenda. EU Agencies are knowledge centres, bringing together know-how to inform policy makers.

Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger.

Benzoate-para-hydroxylase (CYP51A or BpH) and NADPH:cytochrome P450 reductase from the filamentous fungus Aspergillus niger were purified to apparent homogeneity, using an overproducing A. niger strain. This is the first membrane-bound fungal cytochrome P450 to be isolated and characterized.

Constitutive and inducible hydroxylase activities involved in the degradation of naphthalene by Cunninghamella elegans.

The non-ligninolytic fungus Cunninghamella elegans was investigated for its ability to produce naphthalene hydroxylase (NAH) and naphthol hydroxylase (NOH) activities under various conditions. When the organism was cultivated on a rich growth medium, the mycelia exhibited significant constitutive NAH activity in the late exponential growth phase, but not in the early-exponential-growth-phase. On incubating the early-exponential-growth-phase mycelia with naphthalene, NAH activity was increased five-fold; however, this increase did not occur in the presence of the protein synthesis inhibitor cycloheximide.

Regulation of expression of the Aspergillus niger benzoate para-hydroxylase cytochrome P450 system.

Cytochrome P450 enzyme systems are found throughout nature and are involved in many different, often complex, bioconversions. In the endoplasmic reticulum of the filamentous fungus Aspergillus niger a cytochrome P450 enzyme system is present that is capable of the para-hydroxylation of benzoate. The expression of the two genes encoding the components of this system, the cytochrome P450 gene encoding benzoate para-hydroxylase (bphA) and the gene encoding cytochrome P450 reductase (cprA), is inducible by benzoate.

Cytochrome P450 enzyme systems in fungi.

The involvement of cytochrome P450 enzymes in many complex fungal bioconversion processes has been characterized in recent years. Accordingly, there is now considerable scientific interest in fungal cytochrome P450 enzyme systems. In contrast to S.