| 초록 |
It is known that tyrosinases catalyze the hydroxylation of a monophenol and the conversion of an o-diphenol to the corresponding o-quinone. Especially, the enzymes can be involved in the modification of tyrosine residues into 3,4-dihydroxyphenyl-alanine (DOPA) and DOPA/DOPAquinone-derived intermolecular cross-linking (quinone tanning) in marine environment. Here, we firstly over-expressed a Pinctada fucata tyrosinase in E. coli and simply purified the protein using affinity chromatography. Biochemical properties such as kinetic parameters and reaction specificity was investigated. The results showed the potential ability as a new biocatalyst. We expect the enzyme can be used as a significant biocatalytic marine-derived material for biomedical and industrial applications. |
