Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1191561 | Food Chemistry | 2008 | 9 Pages |
Abstract
This paper demonstrates the presence of an active laccase-like enzyme from deepwater pink shrimp (Parapenaeus longirostris) using polyacrylamide gel electrophoresis. This enzyme was found in all anatomical parts of the deepwater pink shrimp, but particularly in the cephalothorax, and became active during the course of storage. Gel staining with laccase-specific substrates such as ADA, DMP and DAB was used to characterize a protein of around 44Â kDa as containing laccase activity. The enzyme was inhibited by a specific inhibitor, CTAB. 4-Hexylresorcinol, a specific inhibitor of polyphenoloxidase (PPO), did not inhibit the laccase-like enzyme. Low concentrations of antioxidants ascorbic acid or sodium metabisulphite were sufficient to inhibit the laccase-like enzyme. ABTS and DMP were subsequently used to characterize the enzyme. Given the evidence of this enzyme in deepwater pink shrimp, new melanosis-inhibiting compounds that are suitable for consumption need to be found to complement specific inhibitors of PPO activity.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Oscar MartÃnez-Alvarez, Pilar Montero, Carmen Gómez-Guillén,