Characterization of phenoloxidase activity of carapace and viscera from cephalothorax of Norway lobster (Nephrops norvegicus)

The characterization of phenoloxidase activity was performed in both carapace and viscera extracts of Norway lobster. Phenoloxidase activity rose with increasing temperature up to 60 °C. The carapace enzymatic extract showed the highest themostability, retaining about 80% of maximum activity at 45 °C and 40% at 65 °C. On the other hand, both enzymatic extracts showed a single peak activity at neutral-slightly alkaline pH and were quite resistant to inactivation at alkaline pH (pH > 8), but phenoloxidase activity became unstable at pH lower than 5.5. The enzymatic extract obtained from viscera showed a higher affinity for catechol (KM 5.97 mM) than carapace extract (KM 19.40 mM). Both mono- and diphenoloxidase activities were found in carapace and viscera. Polyphenoloxidase and converted-hemocyanin into PPO-like enzyme could be the main responsible for these activities.