Protein patterns of carotenoprotein recovered with or without protease from hepatopancreas of Pacific white shrimp are shown in Fig. 2. The apparent molecular weights (MW) of the major protein bands of carotenoprotein recovered without protease were estimated to be 93 and 45 kDa. Proteins with apparent MW of 77, 61, 57, 53, 34 and 32 kDa were also found in the sample. For carotenoprotein extracted with the aid of protease from hepatopancreas, band intensity of protein with MW of 93 kDa was decreased. It was noted that protein with MW of 45 kDa, which was more likely actin, totally disappeared when protease from hepatopancreas was used. The result suggested that actin was susceptible to hydrolysis by protease added. Furthermore, other proteins were also hydrolysed to some degree as evidenced by the decrease in band intensity with coincidental increase in band intensity at dye front Simpson et al. (1993) reported that carontenoproteins recovered from lobster (Homarus americanus) waste with the aid of bovine trypsin had the proteins with MW of 44 and 90 kDa as the major proteins. The MW of carotenoproteins of Homarus gammarus ranged from 48 to 90 kDa