Phenoloxidase activity of hemocyanin in whiteleg shrimp Penaeus vannamei: conversion, characterization of catalytic properties, and role in postmortem melanosis.
Latent phenoloxidase activity of hemocyanin (Hc) in whiteleg shrimp Penaeus vannamei was assayed to determine its potential involvement in postmortem melanosis. Conversion of pure 12-mer, but not 6-mer, hemocyanin to phenoloxidase by endogenous (serine proteinases) and exogenous (SDS) effectors demonstrated the need of complex aggregation for displaying enzyme activity. Because Hc was converted to Hc-phenoloxidase (HcPO) by hemocytes extracts, the mechanism of conversion seems to be the same for polyphenoloxidases. HcPO has similar biochemical and kinetic properties as real polyphenoloxidases and uses mono- and diphenols as substrates. The kinetics of hydroxygenation of monophenols has a lag phase, typical for tyrosinases, contrary to oxidation of diphenols. Regardless of the structure of the substrate, melanin is finally formed. Because of the abundance, distribution, and resistance of Hc to freezing-thawing, involvement of Hc in black spot formation postmortem is suggested. This has important implications for commercialization of shrimp and related seafood.
García-Carreño
Fernando L
FL
BQ Laboratory, CIBNOR, Mar Bermejo 195, Col. Playa Palo de Santa Rita, La Paz, BCS 23090, Mexico. fgarcia@cibnor.mx
Cota
Keni
K
Navarrete Del Toro
María A
MA
D000818:Animals; D006433:Hemocyanins / Q000378:metabolism*; D008543:Melanins / Q000032:analysis / Q000378:metabolism*; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D033561:Penaeidae / Q000201:enzymology*; D010858:Pigmentation; D011180:Postmortem Changes
D008543:Melanins; D006433:Hemocyanins; D014442:Monophenol Monooxygenase