This preliminary study showed that carotenoprotein found in J. lalandii, whilst displaying the characteristic colour changes, appears to have a different composition to that of the blue crustacyanin, including the propensity to convert to the β form. Surprisingly the λmax of the larger molecule was at a lower wave length than that of the smaller molecule suggesting differences in the prosthetic group and the protein. Confirmation of the prosthetic group by NMR, and studies on the protein–carotenoid interactions as carried out by Krawczyk and Britton (2001) could indicate whether the same orientations as found with blue α-crustacyanin pertain. Similarly, separation of the constituent peptides and comparison to the Homarus and Astacus species ( Gomez et al., 1986 and Zagalsky and Tidmarsh, 1985) and analysis of the constituent amino acids ( Keen et al., 1991) could highlight differences in the protein moiety and help explain the different behaviours in low ionic media.
The work suggests the β-complex could be exploited commercially due to its predominance, the ability to undergo reversible colour changes and the apparent stability over a wide range of temperature and pH.