Crosslinking reaction of phenolic side chains in silk fibroin by tyrosinase

Tyrosinase oxidizes the tyrosyl residues in silk fibroin (SF) with oxygen, resulting in the production of o-quinone residues. Subsequently, the inter- or intramolecular crosslinks are formed by reaction with amino groups in through nonenzymatic process. The measurement of oxygen consumption proved that the tyrosyl residues in SF were mostly oxidized to quinone residues by tyrosinase. The reaction mechanisms were proposed in this study and the crosslinking reaction of o-quinone residues and the enzymatic oxidation of tyrosyl residues could be confirmed by the measurements of UV, H-1-NMR and GFC.