Concentration of Zn, Cu, Cd, Pb and Co have been determined in Antarctic water (South Shetland Islands) and in krill exoskeletons with the help of atomic absorption spectrophotometry. Concentrations of these metals both in sea-water and in krill exoskeleton are in order Zn > Cu > Cd > Ni > Pb > Co. Comparing concentrations of these metals in sea-water to their concentrations in krill exoskeleton, the factors have been calculated giving a list of metals in the order of krill chitin ability, which is Ni > Cu > Zn > Cd > Pb > Co accumulation. The highest accumulation factors for Ni and Cu point out to the special role played by these metals in krill life.
The possibility of producing chitosan by enzymatic deacetylation of chitin has been the subject of numerous investigations over the last twenty years, but to date no satisfactory method has been developed. In this paper the influence of chitin chain conformation and chitin particle crystallinity on the enzymatic deacetylation of chitin is investigated to determine the relative importance of these two factors on the process. It is shown that the high crystallinity of chitin is the main obstacle to converting chitin to chitosan by enzymatic deacetylation.
Chitin deacetylase is the only known enzyme which is able to deacetylate N-acetyl-D-glucosamine units in chitin or chitosan chains. As chitin can hardly be dissolved in organic/inorganic solvents, new solvents are still searched. Ionic liquids are promising for that application and for homophase enzymatic deacetylation. The aim of the work was to investigate the influence of selected ionic liquids on activity of chitin deacetylase. It has been shown that [Amim] ionic liquids increase the activity of chitin deacetylase. The highest activity was observed for [Amim][Cl]. Ionic liquids with shorter (ethyl (C2)) and longer side chain (buthyl (C4)) only insignificantly influenced the activity of the enzyme. All tested ionic liquids with [Br] anion increased the activity of chitin deacetylase while the [Emim] and [Bmim] cation in combination with [Cl] anion inhibited the activity of the enzyme.